Trehalose and its applications in the food industry.
food protection
stabilizer
sweetener
trehalose
Journal
Comprehensive reviews in food science and food safety
ISSN: 1541-4337
Titre abrégé: Compr Rev Food Sci Food Saf
Pays: United States
ID NLM: 101305205
Informations de publication
Date de publication:
11 2022
11 2022
Historique:
revised:
29
07
2022
received:
14
04
2022
accepted:
31
08
2022
pubmed:
7
10
2022
medline:
25
11
2022
entrez:
6
10
2022
Statut:
ppublish
Résumé
Trehalose is a nonreducing disaccharide composed of two glucose molecules linked by α, α-1,1-glycosidic bond. It is present in a wide variety of organisms, including bacteria, fungi, insects, plants, and invertebrate animals. Trehalose has distinct physical and chemical properties that have been investigated for their biological importance in a range of prokaryotic and eukaryotic species. Emerging research on trehalose has identified untapped opportunities for its application in the food, medical, pharmaceutical, and cosmetics industries. This review summarizes the chemical and biological properties of trehalose, its occurrence and metabolism in living organisms, its protective role in molecule stabilization, and natural and commercial production methods. Utilization of trehalose in the food industry, in particular how it stabilizes protein, fat, carbohydrate, and volatile compounds, is also discussed in depth. Challenges and opportunities of its application in specific applications (e.g., diagnostics, bioprocessing, ingredient technology) are described. We conclude with a discussion on the potential of leveraging the unique molecular properties of trehalose in molecular stabilization for improving the safety, quality, and sustainability of our food systems.
Identifiants
pubmed: 36201393
doi: 10.1111/1541-4337.13048
doi:
Substances chimiques
Trehalose
B8WCK70T7I
Types de publication
Review
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
5004-5037Informations de copyright
© 2022 Institute of Food Technologists®.
Références
Abbasi, J. (2018). Did a sugar called trehalose contribute to the clostridium difficile epidemic? Journal of the American Medical Association, 319(14), 1425-1426. https://doi.org/10.1001/jama.2018.0888
Aga, H., Shibuya, T., Chaen, H., Fukuda, S., & Kurimoto, M. (1998). Stabilization by trehalose of superoxide dismutase-like activity of various vegetables. Nippon Shokuhin Kagaku Kogaku Kaishi, 45(3), 210-215. https://doi.org/10.3136/nskkk.45.210
Agarwal, N., & Singh, S. P. (2021). A novel trehalose synthase for the production of trehalose and trehalulose. Microbiology Spectrum, 9(3), e0133321. https://doi.org/10.1128/spectrum.01333-21
Aguib, Y., Heiseke, A., Gilch, S., Riemer, C., Baier, M., Schätzl, H. M., & Ertmer, A. (2009). Autophagy induction by trehalose counteracts cellular prion infection. Autophagy, 5(3), 361-369. https://doi.org/10.4161/auto.5.3.7662
Aguilera, J. M. (2019). The food matrix: Implications in processing, nutrition and health. Critical Reviews in Food Science and Nutrition, 59(22), 3612-3629. https://doi.org/10.1080/10408398.2018.1502743
Aisaka, K., Masuda, T., Chikamune, T., & Kamitori, K. (1998). Purification and characterization of trehalose phosphorylase from catellatospora ferruginea. Bioscience, Biotechnology and Biochemistry, 62(4), 782-787. https://doi.org/10.1271/bbb.62.782
Aktas, T., Fujii, S., Kawano, Y., & Yamamoto, S. (2007). Effects of pretreatments of sliced vegetables with trehalose on drying characteristics and quality of dried products. Food and Bioproducts Processing, 85(3C), 178-183. https://doi.org/10.1205/fbp07037
Allison, S. D., Chang, B., Randolph, T. W., & Carpenter, J. F. (1999). Hydrogen bonding between sugar and protein is responsible for inhibition of dehydration-induced protein unfolding. Archives of Biochemistry and Biophysics, 365(2), 289-298. https://doi.org/10.1006/abbi.1999.1175
Almeida, A. M., Cardoso, L. A., Santos, D. M., Torné, J. M., & Fevereiro, P. S. (2007). Trehalose and its applications in plant biotechnology. In Vitro Cellular and Developmental Biology - Plant, 43(3), 167-177. https://doi.org/10.1007/s11627-006-9024-3
Alugupalli, S., Laneelle, M. A., Larsson, L., & Daffe, M. (1995). Chemical characterization of the ester-linked 3-hydroxy fatty acyl- containing lipids in Mycobacterium tuberculosis. Journal of Bacteriology, 177(15), 4566-4570. https://doi.org/10.1128/jb.177.15.4566-4570.1995
Álvarez Cerimedo, M. S., Candal, R. J., & Herrera, M. L. (2014). Physical properties and oxidative status of concentrated-from-fish oils microencapsulated in trehalose/sodium caseinate matrix. Food and Bioprocess Technology, 7(12), 3536-3547. https://doi.org/10.1007/s11947-014-1367-x
Álvarez Cerimedo, M. S., Iriart, C. H., Candal, R. J., & Herrera, M. L. (2010). Stability of emulsions formulated with high concentrations of sodium caseinate and trehalose. Food Research International, 43(5), 1482-1493. https://doi.org/10.1016/j.foodres.2010.04.008
Ansari, A., Jones, C. M., Henry, E. R., Hofrichter, J., & Eaton, W. A. (1992). The role of solvent viscosity in the dynamics of protein conformational changes. Science, 256(5065), 1796-1798. https://doi.org/10.1126/science.1615323
Arakawa, T., & Timasheff, S. N. (1982). Stabilization of protein structure by sugars. Biochemistry, 21(25), 6536-6544. https://doi.org/10.1021/bi00268a033
Avonce, N., Mendoza-Vargas, A., Morett, E., & Iturriag, G. (2006). Insights on the evolution of trehalose biosynthesis. BMC Evolutionary Biology, 6, 109. https://doi.org/10.1186/1471-2148-6-109
Babić, J., Šubarić, D., Miličević, B., Ačkar, Đ., Kopjar, M., & Tiban, N. N. (2009). Influence of trehalose, glucose, fructose and sucrose on gelatinization and retrogradation of corn and tapioca starch. Czech Journal of Food Sciences, 27(3), 151-157.
Bai, J., Bai, S., Ren, L., Zhu, K., Zhao, Y., Li, X., & Yuan, X. (2021). Trehalose-modified poly(vinyl alcohol) and their antifogging/antifrosting coatings. Gaodeng Xuexiao Huaxue Xuebao/Chemical Journal of Chinese Universities, 42(8), 2683-2688. https://doi.org/10.7503/cjcu20210060
Bakaltcheva, I., O'Sullivan, A. M., Hmel, P., & Ogbu, H. (2007). Freeze-dried whole plasma: Evaluating sucrose, trehalose, sorbitol, mannitol and glycine as stabilizers. Thrombosis Research, 120(1). https://doi.org/10.1016/j.thromres.2006.07.005
Barrera, C., Burca, C., Betoret, E., García-Hernández, J., Hernández, M., & Betoret, N. (2019). Improving antioxidant properties and probiotic effect of clementine juice inoculated with Lactobacillus salivarius spp. salivarius (CECT 4063) by trehalose addition and/or sublethal homogenisation. International Journal of Food Science and Technology, 54(6), 2109-2122. https://doi.org/10.1111/ijfs.14116
Becker, A., Schlöder, P., Steele, J. E., & Wegener, G. (1996). The regulation of trehalose metabolism in insects. Experientia, 52(5), 433-439. https://doi.org/10.1007/BF01919312
Belton, P. S., & Gil, A. M. (1994). IR and Raman spectroscopic studies of the interaction of trehalose with hen egg white lysozyme. Biopolymers, 34(7), 957-961. https://doi.org/10.1002/bip.360340713
Beltran, F. F., Castillo, R., Vicente-Soler, J., Cansado, J., & Gacto, M. (2000). Role for trehalase during germination of spores in the fission yeast Schizosaccharomyces pombe. FEMS Microbiology Letters, 193(1), 117-121. https://doi.org/10.1016/S0378-1097(00)00471-7
Bergoz, R. (1971). Trehalose malabsorption causing intolerance to mushrooms. Gastroenterology, 60(5), 909-912. https://doi.org/10.1016/s0016-5085(71)80092-6
Betoret, E., Calabuig-Jiménez, L., Patrignani, F., Lanciotti, R., & Dalla Rosa, M. (2017). Effect of high pressure processing and trehalose addition on functional properties of mandarin juice enriched with probiotic microorganisms. LWT - Food Science and Technology, 85, 418-422. https://doi.org/10.1016/j.lwt.2016.10.036
Betoret, E., Mannozzi, C., Dellarosa, N., Laghi, L., Rocculi, P., & Dalla Rosa, M. (2017). Metabolomic studies after high pressure homogenization processed low pulp mandarin juice with trehalose addition. Functional and technological properties. Journal of Food Engineering, 200, 22-28. https://doi.org/10.1016/j.jfoodeng.2016.12.011
Bhandal, I. S., Hauptmann, R. M., & Widholm, J. M. (1985). Trehalose as cryoprotectant for the freeze preservation of carrot and tobacco cells. Plant Physiology, 78(2), 430-432. https://doi.org/10.1104/pp.78.2.430
Boehnke, N., Kammeyer, J. K., Damoiseaux, R., & Maynard, H. D. (2018). Stabilization of glucagon by trehalose glycopolymer nanogels. Advanced Functional Materials, 28(10), 1705475. https://doi.org/10.1002/adfm.201705475
Bolte, J. P., Schönhage, F., Förster, E., Knolle, J., & Meyer zum Büschenfelde, K. H. (1973). Zur diagnostischen Bedeutung der Trehalose-Belastung bei Malassimilationssyndromen. Deutsche Medizinische Wochenschrift, 98(28), 1303-1307. https://doi.org/10.1055/s-0028-1107030
Brennan, P. J., & Nikaido, H. (1995). The envelope of mycobacteria. Annual Review of Biochemistry, 64, 29-63. https://doi.org/10.1146/annurev.bi.64.070195.000333
Buckley, A. M., Moura, I. B., Arai, N., Spittal, W., Clark, E., Nishida, Y., Harris, H. C., Bentley, K., Davis, G., Wang, D., Mitra, S., Higashiyama, T., & Wilcox, M. H. (2021). Trehalose-induced remodelling of the human microbiota affects Clostridioides difficile infection outcome in an in vitro colonic model: A pilot study. Frontiers in Cellular and Infection Microbiology, 11, 670935. https://doi.org/10.3389/fcimb.2021.670935
Cabib, E., & Leloir, L. F. (1958). The biosynthesis of trehalose phosphate. The Journal of Biological Chemistry, 231(1), 259-275. https://doi.org/10.1016/s0021-9258(19)77303-7
Caffrey, M. (1987). The combined and separate effects of low temperature and freezing on membrane lipid mesomorphic phase behavior: Relevance to cryobiology. BBA - Biomembranes, 896(1), 123-127. https://doi.org/10.1016/0005-2736(87)90365-8
Cai, X., Seitl, I., Mu, W., Zhang, T., Stressler, T., Fischer, L., & Jiang, B. (2018). Biotechnical production of trehalose through the trehalose synthase pathway: Current status and future prospects. Applied Microbiology and Biotechnology, 102(7), 2965-2976. https://doi.org/10.1007/s00253-018-8814-y
Candy, D. J., & Kilby, B. A. (1959). Site and mode of trehalose biosynthesis in the locust. Nature, 183(4675), 1594-1595. https://doi.org/10.1038/1831594a0
Carpenter, J. F., & Crowe, J. H. (1989). An infrared spectroscopic study of the interactions of carbohydrates with dried proteins. Biochemistry, 28(9), 3916-3922. https://doi.org/10.1021/bi00435a044
Castillo, K., Nassif, M., Valenzuela, V., Rojas, F., Matus, S., Mercado, G., Court, F. A., van Zundert, B., & Hetz, C. (2013). Trehalose delays the progression of amyotrophic lateral sclerosis by enhancing autophagy in motoneurons. Autophagy, 9(9), 1308-1320. https://doi.org/10.4161/auto.25188
Čejková, J., Čejka, C., Ardan, T., Širc, J., Michálek, J., & Luyckx, J. (2010). Reduced UVB-induced corneal damage caused by reactive oxygen and nitrogen species and decreased changes in corneal optics after trehalose treatment. Histology and Histopathology, 25(11), 1403-1416. https://doi.org/10.14670/HH-25.1403
Chaen, H., Nakada, T., Nishimoto, T., Kuroda, N., Fukuda, S., Sugimoto, T., Kurimoto, M., & Tsujisaka, Y. (1999). Purification and characterization of thermostable trehalose phosphorylase from Thermoanaerobium brockii. Journal of Applied Glycoscience, 46(4), 399-405. https://doi.org/10.5458/jag.46.399
Chaitanya, S. N. N., Devi, A., Sahu, S., & Alugoju, P. (2021). Molecular mechanisms of action of Trehalose in cancer: A comprehensive review. Life Sciences, 269, 118968. https://doi.org/10.1016/j.lfs.2020.118968
Chao, X., Bin, Z., Lu-Kai, M., & Ji-Peng, S. (2017). Cryoprotective effects of trehalose, alginate, and its oligosaccharide on quality of cooked-shrimp (Litopenaeus vannamei) during frozen storage. Journal of Food Processing and Preservation, 41(2), e12825. https://doi.org/10.1111/jfpp.12825
Chen, H., Wu, F., Duan, X., Yang, N., Xu, Y., Xu, B., Jin, Z., & Xu, X. (2013). Characterization of emulsions prepared by egg yolk phosvitin with pectin, glycerol and trehalose. Food Hydrocolloids, 30(1), 123-129. https://doi.org/10.1016/j.foodhyd.2012.05.007
Clegg, J. S. (1965). The origin of threhalose and its significance during the formation of encysted dormant embryos of Artmia salina. Comparative Biochemistry And Physiology, 135-143. https://doi.org/10.1016/0010-406X(65)90014-9
Colaço, C., & Roser, B. (2011). Trehalose-a multifunctional additive for food preservation. In Food Packaging and Preservation (pp. 123-140). Springer US. https://doi.org/10.1007/978-1-4615-2173-0_7
Colaço, C., Sen, S., Thangavelu, M., Pinder, S., & Roser, B. (1992). Extraordinary stability of enzymes dried in trehalose: Simplified molecular biology. Bio/Technology, 10(9), 1007-1011. https://doi.org/10.1038/nbt0992-1007
Collins, J., Robinson, C., Danhof, H., Knetsch, C. W., van Leeuwen, H. C., Lawley, T. D., Auchtung, J. M., & Britton, R. A. (2018). Dietary trehalose enhances virulence of epidemic Clostridium difficile. Nature, 553(7688), 291-294. https://doi.org/10.1038/nature25178
Conrad, P. B., & de Pablo, J. J. (1999). Computer simulation of the cryoprotectant disaccharide α,α-trehalose in aqueous solution. Journal of Physical Chemistry A, 103(20), 4049-4055. https://doi.org/10.1021/jp984102b
Crowe, J. H. (2007). Trehalose as a “chemical chaperone”: Fact and fantasy. Advances in Experimental Medicine and Biology, 594, 143-158. https://doi.org/10.1007/978-0-387-39975-1_13
Crowe, J. H., Carpenter, J. F., & Crowe, L. M. (1998). The role of vitrification in anhydrobiosis. Annual Review of Physiology, 60, 73-103. https://doi.org/10.1146/annurev.physiol.60.1.73
Crowe, J. H., Crowe, L. M., & Chapman, D. (1984). Preservation of membranes in anhydrobiotic organisms: The role of trehalose. Science, 223(4637), 701-703. https://doi.org/10.1126/science.223.4637.701
Crowe, J. H., Crowe, L. M., & Mouradian, R. (1983). Stabilization of biological membranes at low water activities. Cryobiology, 20(3), 346-356. https://doi.org/10.1016/0011-2240(83)90023-8
Crowe, J. H., Hoekstra, F. A., Nguyen, K. H. N., & Crowe, L. M. (1996). Is vitrification involved in depression of the phase transition temperature in dry phospholipids? Biochimica et Biophysica Acta - Biomembranes, 1280(2), 187-196. https://doi.org/10.1016/0005-2736(95)00287-1
Daffé, M., Lacave, C., Lanéelle, M., Gillois, M., & Lanéelle, G. (1988). Polyphthienoyl trehalose, glycolipids specific for virulent strains of the tubercle bacillus. European Journal of Biochemistry, 172(3), 579-584. https://doi.org/10.1111/j.1432-1033.1988.tb13928.x
Dahlqvist, A. (1962). Specificity of the human intestinal disaccharidases and implications for hereditary disaccharide intolerance. Journal of Clinical Investigation, 41(3), 463-470. https://doi.org/10.1172/jci104499
Dashnau, J. L., Sharp, K. A., & Vanderkooi, J. M. (2005). Carbohydrate intramolecular hydrogen bonding cooperativity and its effect on water structure. Journal of Physical Chemistry B, 109(50), 24152-24159. https://doi.org/10.1021/jp0543072
de Virgilio, C., Bürckert, N., Bell, W., Jenö, P., Boller, T., & Wiemken, A. (1993). Disruption of TPS2, the gene encoding the 100-kDa subunit of the trehalose-6-phosphate synthase/phosphatase complex in Saccharomyces cerevisiae, causes accumulation of trehalose-6-phosphate and loss of trehalose-6-phosphate phosphatase activity. European Journal of Biochemistry, 212(2), 315-323. https://doi.org/10.1111/j.1432-1033.1993.tb17664.x
Debnath, K., Pradhan, N., Singh, B. K., Jana, N. R., & Jana, N. R. (2017). Poly(trehalose) nanoparticles prevent amyloid aggregation and suppress polyglutamine aggregation in a Huntington's disease model mouse. ACS Applied Materials and Interfaces, 9(28), 24126-24129. https://doi.org/10.1021/acsami.7b06510
Domian, E., Brynda-Kopytowska, A., Cenkier, J., & Wirydow, E. (2015). Selected properties of microencapsulated oil powders with commercial preparations of maize OSA starch and trehalose. Journal of Food Engineering, 152, 72-84. https://doi.org/10.1016/j.jfoodeng.2014.09.034
Domian, E., Brynda-Kopytowska, A., & Marzec, A. (2017). Functional properties and oxidative stability of flaxseed oil microencapsulated by spray drying using legume proteins in combination with soluble fiber or trehalose. Food and Bioprocess Technology, 10(7), 1374-1386. https://doi.org/10.1007/s11947-017-1908-1
Domínguez, R., Pateiro, M., Gagaoua, M., Barba, F. J., Zhang, W., & Lorenzo, J. M. (2019). A comprehensive review on lipid oxidation in meat and meat products. Antioxidants, 8(10), 429. https://doi.org/10.3390/antiox8100429
Doran, P. M., & Bailey, J. E. (1986). Effects of immobilization on growth, fermentation properties, and macromolecular composition of Saccharomyces cerevisiae attached to gelatin. Biotechnology and Bioengineering, 28(1), 73-87. https://doi.org/10.1002/bit.260280111
Drusch, S., Serfert, Y., van den Heuvel, A., & Schwarz, K. (2006). Physicochemical characterization and oxidative stability of fish oil encapsulated in an amorphous matrix containing trehalose. Food Research International, 39(7), 807-815. https://doi.org/10.1016/j.foodres.2006.03.003
Eis, C., & Nidetzky, B. (1999). Characterization of trehalose phosphorylase from Schizophyllum commune. Biochemical Journal, 341(2), 385-393. https://doi.org/10.1042/0264-6021:3410385
Ekdawi-Sever, N., Conrad, P. B., & de Pablo, J. J. (2001). Molecular simulation of sucrose solutions near the glass transition temperature. Journal of Physical Chemistry A, 105(4), 734-742. https://doi.org/10.1021/jp002722i
Ekdawi-Sever, N., de Pablo, J. J., Feick, E., & von Meerwall, E. (2003). Diffusion of sucrose and α,α-trehalose in aqueous solutions. Journal of Physical Chemistry A, 107(6), 936-943. https://doi.org/10.1021/jp020187b
Elbein, A. D. (1968). Trehalose phosphate synthesis in Streptomyces hygroscopicus: Purification of guanosine diphosphate D-glucose: D-glucose-6-phosphate 1-glucosyl-transferase. Journal of Bacteriology, 96(5), 1623-1631. https://doi.org/10.1128/jb.96.5.1623-1631.1968
Elbein, A. D. (1974). The metabolism of α,α-trehalose. Advances in Carbohydrate Chemistry and Biochemistry, 227-256. https://doi.org/10.1016/S0065-2318(08)60266-8
Elbein, A. D., Pan, Y. T., Pastuszak, I., & Carroll, D. (2003). New insights on trehalose: A multifunctional molecule. Glycobiology, 17R-27R. https://doi.org/10.1093/glycob/cwg047
Eleutherio, E. (2018). Trehalose: As sweet as effective in biomedical research and biotechnology. Advances in Biotechnology & Microbiology, 8(4), 555745. https://doi.org/10.19080/aibm.2018.08.555745
Eleutherio, E., Panek, A., de Mesquita, J. F., Trevisol, E., & Magalhães, R. (2015). Revisiting yeast trehalose metabolism. Current Genetics, 61(3), 263-274. https://doi.org/10.1007/s00294-014-0450-1
Erkut, C., Penkov, S., Khesbak, H., Vorkel, D., Verbavatz, J. M., Fahmy, K., & Kurzchalia, T. (2011). Trehalose renders the dauer larva of caenorhabditis elegans resistant to extreme desiccation. Current Biology, 21(15), 1331-1336. https://doi.org/10.1016/j.cub.2011.06.064
Evans, D. R., & Dethier, V. G. (1957). The regulation of taste thresholds for sugars in the blowfly. Journal of Insect Physiology, 1(1), 3-17. https://doi.org/10.1016/0022-1910(57)90019-7
Eyre, D. W., Didelot, X., Buckley, A. M., Freeman, J., Moura, I. B., Crook, D. W., Peto, T. E. A., Walker, A. S., Wilcox, M. H., & Dingle, K. E. (2019). Clostridium difficile trehalose metabolism variants are common and not associated with adverse patient outcomes when variably present in the same lineage. EBioMedicine, 43, 347-355. https://doi.org/10.1016/j.ebiom.2019.04.038
Feofilova, E. P., Usov, A. I., Mysyakina, I. S., & Kochkina, G. A. (2014). Trehalose: Chemical structure, biological functions, and practical application. Microbiology (Russian Federation), 83(3), 184-194. https://doi.org/10.1134/S0026261714020064
Fernandes, P. M. B., Farina, M., & Kurtenbach, E. (2001). Effect of hydrostatic pressure on the morphology and ultrastructure of wild-type and trehalose synthase mutant cells of Saccharomyces cerevisiae. Letters in Applied Microbiology, 32(1), 42-46. https://doi.org/10.1046/j.1472-765X.2001.00853.x
Foster, A. J., Jenkinson, J. M., & Talbot, N. J. (2003). Trehalose synthesis and metabolism are required at different stages of plant infection by Magnaporthe grisea. EMBO Journal, 22(2), 225-235. https://doi.org/10.1093/emboj/cdg018
Friedman, S. (1960). The purification and properties of trehalase isolated from Phormia regina, Meig. Archives of Biochemistry and Biophysics, 87(2), 252-258. https://doi.org/10.1016/0003-9861(60)90169-7
Fu, Z., Chen, J., Luo, S. J., Liu, C. M., & Liu, W. (2015). Effect of food additives on starch retrogradation: A review. Starch/Staerke, 67(1-2), 69-78. https://doi.org/10.1002/star.201300278
Fuchigami, M., Ogawa, N., & Teramoto, A. (2002). Trehalose and hydrostatic pressure effects on the structure and sensory properties of frozen tofu (soybean curd). Innovative Food Science and Emerging Technologies, 3(2), 139-147. https://doi.org/10.1016/S1466-8564(02)00007-3
Galand, G. (1989). Brush border membrane sucrase-isomaltase, maltase-glucoamylase and trehalase in mammals. Comp. Biochem. Physiol. B, 94(1), 1-11.
Galinski, E. A. (1993). Compatible solutes of halophilic eubacteria: Molecular principles, water-solute interaction, stress protection. Experientia, 49(6-7), 487-496. https://doi.org/10.1007/BF01955150
Galmarini, M. v., Schebor, C., Zamora, M. C., & Chirife, J. (2009). The effect of trehalose, sucrose and maltodextrin addition on physicochemical and sensory aspects of freeze - dried strawberry puree. International Journal of Food Science and Technology, 44(10), 1869-1876. https://doi.org/10.1111/j.1365-2621.2008.01890.x
Galmarini, M. v., van Baren, C., Zamora, M. C., Chirife, J., di Leo Lira, P., & Bandoni, A. (2011). Impact of trehalose, sucrose and/or maltodextrin addition on aroma retention in freeze dried strawberry puree. International Journal of Food Science and Technology, 1337-1345. https://doi.org/10.1111/j.1365-2621.2011.02598.x
Garg, A. K., Kim, J. K., Owens, T. G., Ranwala, A. P., do Choi, Y., Kochian, L. v., & Wu, R. J. (2002). Trehalose accumulation in rice plants confers high tolerance levels to different abiotic stresses. Proceedings of the National Academy of Sciences of the United States of America, 99(25), 15898-15903. https://doi.org/10.1073/pnas.252637799
Gerardo-Rodríguez, J. E., Ramírez-Wong, B., Ledesma-Osuna, A. I., Medina-Rodríguez, C. L., Ortega-Ramírez, R., & Silvas-García, M. I. (2017). Management of freezing rate and trehalose concentration to improve frozen dough properties and bread quality. Food Science and Technology, 37(1), 59-64. https://doi.org/10.1590/1678-457X.00482
Giaever, H. M., Styrvold, O. B., Kaasen, I., & Strøm, A. R. (1988). Biochemical and genetic characterization of osmoregulatory trehalose synthesis in Escherichia coli. Journal of Bacteriology, 170(6), 2841-2849. https://doi.org/10.1128/jb.170.6.2841-2849.1988
Giannou, V., & Tzia, C. (2008). Cryoprotective role of exogenous trehalose in frozen dough products. Food and Bioprocess Technology, 1(3), 276-284. https://doi.org/10.1007/s11947-007-0008-z
Gibney, P. A., Schieler, A., Chen, J. C., Rabinowitz, J. D., & Botstein, D. (2015). Characterizing the in vivo role of trehalose in Saccharomyces cerevisiae using the AGT1 transporter. Proceedings of the National Academy of Sciences, 112(19), 6116 LP-6121. https://doi.org/10.1073/pnas.1506289112
Goff, D. (1992). Low-temperature stability and the glassy state in frozen foods. Food Research International, 25(4), 317-325. https://doi.org/10.1016/0963-9969(92)90128-R
Golon, A., Kropf, C., Vockenroth, I., & Kuhnert, N. (2014). An investigation of the complexity of maillard reaction product profiles from the thermal reaction of amino acids with sucrose using high resolution mass spectrometry. Foods, 3(3), 461-475. https://doi.org/10.3390/foods3030461
Gudmand-Høsyer, E., Fenger, H. J., Skovbjerg, H., Kern-Hansen, P., & Madsen, P. R. (1988). Trehalase deficiency in Greenland. Scandinavian Journal of Gastroenterology, 23(7), 775-778. https://doi.org/10.3109/00365528809090759
Guo, N., Puhlev, I., Brown, D. R., Mansbridge, J., & Levine, F. (2000). Trehalose expression confers desiccation tolerance on human cells. Nature Biotechnology, 18(2), 168-171. https://doi.org/10.1038/72616
Hagen, S. J., Hofrichter, J., & Eaton, W. A. (1995). Protein reaction kinetics in a room-temperature glass. Science, 269(5226), 959-962. https://doi.org/10.1126/science.7638618
Halagarda, M. (2017). Effects of trehalose and dough additives incorporating enzymes on physical characteristics and sensory properties of frozen savory Danish dough. LWT - Food Science and Technology, 86, 603-610. https://doi.org/10.1016/j.lwt.2017.08.048
Han, S. E., Kwon, H., Lee, S. B., Yi, B. Y., Murayama, I., Kitamoto, Y., & Byun, M. O. (2003). Cloning and characterization of a gene encoding trehalose phosphorylase (TP) from Pleurotus sajor-caju. Protein Expression and Purification, 30(2), 194-202. https://doi.org/10.1016/S1046-5928(03)00104-9
Haque, M. A., Chen, J., Aldred, P., & Adhikari, B. (2015). Drying and denaturation characteristics of whey protein isolate in the presence of lactose and trehalose. Food Chemistry, 177, 8-16. https://doi.org/10.1016/j.foodchem.2014.12.064
He, Q., Koprich, J. B., Wang, Y., Yu, W., Xiao, B., Brotchie, J. M., & Wang, J. (2016). Treatment with trehalose prevents behavioral and neurochemical deficits produced in an AAV α-Synuclein rat model of Parkinson's disease. Molecular Neurobiology, 53(4), 2258-2268. https://doi.org/10.1007/s12035-015-9173-7
Helferich, B., & Weis, K. (1956). Zur Synthese von Glucosiden und von nicht-reduzierenden Disacchariden. Chemische Berichte, 89(2), 314-321. https://doi.org/10.1002/cber.19560890220
Hengge-Aronis, R., Klein, W., Lange, R., Rimmele, M., & Boos, W. (1991). Trehalose synthesis genes are controlled by the putative sigma factor encoded by rpoS and are involved in stationary-phase thermotolerance in Escherichia coli. Journal of Bacteriology, 173(24), 7918-7924. https://doi.org/10.1128/jb.173.24.7918-7924.1991
Herdeiro, R. S., Pereira, M. D., Panek, A. D., & Eleutherio, E. C. A. (2006). Trehalose protects Saccharomyces cerevisiae from lipid peroxidation during oxidative stress. Biochimica et Biophysica Acta - General Subjects, 1760(3), 340-346. https://doi.org/10.1016/j.bbagen.2006.01.010
Higashiyama, T. (2002). Novel functions and applications of trehalose. Pure and Applied Chemistry, 74(7), 1263-1269. https://doi.org/10.1351/pac200274071263
Himei, S. (2008). New developments in the use of Treha(R) in the food industry. Food Chem, 7, 25-29.
Hirata, T. (2009). Effects of trehalose on texture of cooked rice. Bulletin of Hiroshima Prefectural Technology Research Institute Food Technology Research Center, 25, 1-4.
Holler, C. J., Taylor, G., McEachin, Z. T., Deng, Q., Watkins, W. J., Hudson, K., Easley, C. A., Hu, W. T., Hales, C. M., Rossoll, W., Bassell, G. J., & Kukar, T. (2016). Trehalose upregulates progranulin expression in human and mouse models of GRN haploinsufficiency: A novel therapeutic lead to treat frontotemporal dementia. Molecular Neurodegeneration, 11(1), 46. https://doi.org/10.1186/s13024-016-0114-3
Hottiger, T., Boller, T., & Wiemken, A. (1987). Rapid changes of heat and desiccation tolerance correlated with changes of trehalose content in Saccharomyces cerevisiae cells subjected to temperature shifts. FEBS Letters, 220(1), 113-115. https://doi.org/10.1016/0014-5793(87)80886-4
Ichihara, H., Kuwabara, K., & Matsumoto, Y. (2017). Trehalose liposomes suppress the growth of tumors on human lung carcinoma-bearing mice by induction of apoptosis in vivo. Anticancer Research, 37(11), 6133-6139. https://doi.org/10.21873/anticanres.12062
Inoue, Y., Ishii, K., Tomita, T., Yatake, T., & Fukui, F. (2002). Characterization of trehalose phosphorylase from bacillus stearothermophilus sk-1 and nucleotide sequence of the corresponding gene. Bioscience, Biotechnology and Biochemistry, 66(9), 1835-1843. https://doi.org/10.1271/bbb.66.1835
Iordachescu, M., & Imai, R. (2011). Trehalose and abiotic stress in biological systems. In (A. K. Shanker Ed.), Abiotic stress in plants - mechanisms and adaptations. IntechOpen. https://doi.org/10.5772/22208
Iturriaga, G., Gaff, D. F., & Zentella, R. (2000). New desiccation-tolerant plants, including a grass, in the central highlands of Mexico, accumulate trehalose. Australian Journal of Botany, 48(2), 153-158. https://doi.org/10.1071/BT98062
Iturriaga, G., Suárez, R., & Nova-Franco, B. (2009). Trehalose metabolism: From osmoprotection to signaling. International Journal of Molecular Sciences, 10(9), 3793-3810. https://doi.org/10.3390/ijms10093793
Jain, N. K., & Roy, I. (2009). Effect of trehalose on protein structure. Protein Science, 18(1), 24-36. https://doi.org/10.1002/pro.3
Jothi, J. S., Le, T. N. D., & Kawai, K. (2020). Effects of trehalose and corn starch on the mechanical glass transition temperature and texture properties of deep-fried food with varying water and oil contents. Journal of Food Engineering, 267, 109731. https://doi.org/10.1016/j.jfoodeng.2019.109731
Kalf, G. F., & Rieder, S. V. (1958). The purification and properties of trehalase. The Journal of Biological Chemistry, 230(2), 252-258. https://doi.org/10.1016/s0021-9258(18)70491-2
Kandror, O., DeLeon, A., & Goldberg, A. L. (2002). Trehalose synthesis is induced upon exposure of Escherichia coli to cold and is essential for viability at low temperatures. Proceedings of the National Academy of Sciences of the United States of America, 99(15), 9727-9732. https://doi.org/10.1073/pnas.142314099
Kang, H. J., Kim, S. H., & Lim, J. K. (2010). Effect of trehalose on moisture and texture characteristics of instant Baekseolgi prepared by microwave oven. Korean Journal of Food Science and Technology, 42(3), 304-309.
Kanner, J. (2007). Dietary advanced lipid oxidation end products are risk factors to human health. Molecular Nutrition and Food Research, 51(9), 1094-1101. https://doi.org/10.1002/mnfr.200600303
Khalifeh, M., Barreto, G. E., & Sahebkar, A. (2019). Trehalose as a promising therapeutic candidate for the treatment of Parkinson's disease. British Journal of Pharmacology, 176(9), 1173-1189. https://doi.org/10.1111/bph.14623
Khalifeh, M., Read, M. I., Barreto, G. E., & Sahebkar, A. (2020). Trehalose against Alzheimer's disease: Insights into a potential therapy. BioEssays, 42(8), e1900195. https://doi.org/10.1002/bies.201900195
Kim, S. S., & Chung, H. Y. (2009). Quality characteristics of a Korean rice cake (Karedduk) with mixture of trehalose and modified starch by using response surface methodology. Journal of the Korean Society of Food Science and Nutrition, 38(3), 377-383. https://doi.org/10.3746/jkfn.2009.38.3.377
Kim, T. K., Jang, J. H., Cho, H. Y., Lee, H. S., & Kim, Y. W. (2010). Gene cloning and characterization of a trehalose synthase from corynebacterium glutamicum ATCC13032. Food Science and Biotechnology, 19(2), 565-569. https://doi.org/10.1007/s10068-010-0079-x
Kim, Y. J., Lee, J. H., Chung, K. C., & Lee, S. K. (2014a). Effect of trehalose on rheological properties of bread flour dough. Korean Journal of Food Science and Technology, 46(3), 341-346. https://doi.org/10.9721/KJFST.2014.46.3.341
Kim, Y. J., Lee, J. H., Chung, K. C., & Lee, S. K. (2014b). Effects of trehalose on quality characteristics of white pan bread. Journal of the Korean Society of Food Science and Nutrition, 43(5), 712-719. https://doi.org/10.3746/jkfn.2014.43.5.712
Kim, Y. S., Huang, W., Du, G., Pan, Z., & Chung, O. (2008). Effects of trehalose, transglutaminase, and gum on rheological, fermentation, and baking properties of frozen dough. Food Research International, 41(9), 903-908. https://doi.org/10.1016/j.foodres.2008.07.013
Kita, Y., Arakawa, T., Lin, T., & Timasheff, S. N. (1994). Contribution of the surface free energy perturbation to protein-solvent interactions. Biochemistry, 33(50), 15178-15189. https://doi.org/10.1021/bi00254a029
Komes, D., Lovrić, T., Ganić, K. K., & Gracin, L. (2003). Study of trehalose addition on aroma retention in dehydrated strawberry puree. Food Technology and Biotechnology, 111-119.
Komes, D., Lovrić, T., Ganić, K. K., Kljusurić, J. G., & Banović, M. (2005). Trehalose improves flavour retention in dehydrated apricot puree. International Journal of Food Science and Technology, 40(4), 425-435. https://doi.org/10.1111/j.1365-2621.2005.00967.x
Komes, D., Lovrić, T., & Kovačević Ganić, K. (2007). Aroma of dehydrated pear products. LWT - Food Science and Technology, 40(9), 1578-1586. https://doi.org/10.1016/j.lwt.2006.12.011
Kopjar, M., Hribar, J., Simčič, M., Zlatić, E., Požrl, T., & Piližota, V. (2013). Effect of trehalose addition on volatiles responsible for strawberry aroma. Natural Product Communications, 8(12), 1767-1770. https://doi.org/10.1177/1934578X1300801229
Kopjar, M., Pichler, A., Turi, J., & Piližota, V. (2016). Influence of trehalose addition on antioxidant activity, colour and texture of orange jelly during storage. International Journal of Food Science and Technology, 51(12), 2640-2646. https://doi.org/10.1111/ijfs.13250
Kouril, T., Zaparty, M., Marrero, J., Brinkmann, H., & Siebers, B. (2008). A novel trehalose synthesizing pathway in the hyperthermophilic Crenarchaeon Thermoproteus tenax: The unidirectional TreT pathway. Archives of Microbiology, 190(3), 355-369. https://doi.org/10.1007/s00203-008-0377-3
Kovačević, D., & Mastanjević, K. (2011). Cryoprotective effect of trehalose and maltose on washed and frozen stored beef meat. Czech Journal of Food Sciences, 29(1), 15-23. https://doi.org/10.17221/1042-cjfs
Kovačević, D., & Mastanjević, K. (2014). Cryoprotective effect of trehalose on washed chicken meat. Journal of Food Science and Technology, 51(5), 1006-1010. https://doi.org/10.1007/s13197-011-0553-3
Kubota, M. (2005). New features and properties of trehalose. New Food Industry, 47(3), 17-29.
Kubota, M., Sawatani, I., Oku, K., Takeuchi, K., & Murai, S. (2004). The development of alpha, alpha-trehalose production and its applications. Journal of Applied Glycoscience, 51(1), 63-70. https://doi.org/10.5458/jag.51.63
Landikhovskaya, A. v., Tvorogova, A. A., Kazakova, N. v., & Gursky, I. A. (2020). The effect of trehalose on dispersion of ice crystals and consistency of low-fat ice cream. Food Processing: Techniques and Technology, 50(3), 450-459. https://doi.org/10.21603/2074-9414-2020-3-450-459
Lau, U. Y., Pelegri-O'Day, E. M., & Maynard, H. D. (2018). Synthesis and biological evaluation of a degradable trehalose glycopolymer prepared by RAFT polymerization. Macromolecular Rapid Communications, 39(5), 1700652. https://doi.org/10.1002/marc.201700652
Lederer, E. (1976). Cord factor and related trehalose esters. Chemistry and Physics of Lipids, 16(2), 91-106. https://doi.org/10.1016/0009-3084(76)90001-3
Lee, J., Ko, J. H., Lin, E. W., Wallace, P., Ruch, F., & Maynard, H. D. (2015). Trehalose hydrogels for stabilization of enzymes to heat. Polymer Chemistry, 6(18), 3443-3448. https://doi.org/10.1039/c5py00121h
Lee, J., Lin, E. W., Lau, U. Y., Hedrick, J. L., Bat, E., & Maynard, H. D. (2013). Trehalose glycopolymers as excipients for protein stabilization. Biomacromolecules, 14(8), 2561-2569. https://doi.org/10.1021/bm4003046
Leslie, S. B., Israeli, E., Lighthart, B., Crowe, J. H., & Crowe, L. M. (1995). Trehalose and sucrose protect both membranes and proteins in intact bacteria during drying. Applied and Environmental Microbiology, 61(10), 3592-3597. https://doi.org/10.1128/aem.61.10.3592-3597.1995
Lessa, F. C., Mu, Y., Bamberg, W. M., Beldavs, Z. G., Dumyati, G. K., Dunn, J. R., Farley, M. M., Holzbauer, S. M., Meek, J. I., Phipps, E. C., Wilson, L. E., Winston, L. G., Cohen, J. A., Limbago, B. M., Fridkin, S. K., Gerding, D. N., & McDonald, L. C. (2015). Burden of Clostridium difficile Infection in the United States. New England Journal of Medicine, 372(9), 825-834. https://doi.org/10.1056/nejmoa1408913
Lin, T. Y., & Timasheff, S. N. (1996). On the role of surface tension in the stabilization of globular proteins. Protein Science, 5(2), 372-381. https://doi.org/10.1002/pro.5560050222
Littman, A., & Hammond, J. B. (1965). Diarrhea in adults caused by deficiency in intestinal disaccharidases. Gastroenterology, 48(2), 237-249. https://doi.org/10.1016/S0016-5085(65)80143-3
Liu, X., Xiong, G., Wang, X., Shi, L., Jiao, C., Wu, W., Li, X., Wang, J., Qiao, Y., Liao, L., Ding, A., & Wang, L. (2019). Quality changes of prepared weever (Micropterus salmoides) by base trehalose solution during repeated freeze-thaw cycles. Journal of Food Processing and Preservation, 43(10), e14117. https://doi.org/10.1111/jfpp.14117
Liu, Y., Lee, J., Mansfield, K. M., Ko, J. H., Sallam, S., Wesdemiotis, C., & Maynard, H. D. (2017). Trehalose glycopolymer enhances both solution stability and pharmacokinetics of a therapeutic protein. Bioconjugate Chemistry, 28(3), 836-845. https://doi.org/10.1021/acs.bioconjchem.6b00659
Loncaric, A., Dugalic, K., Mihaljevic, I., Jakobek, L., & Pilizota, V. (2014). Effects of sugar addition on total polyphenol content and antioxidant activity of frozen and freeze-dried apple Purée. Journal of Agricultural and Food Chemistry, 62(7), 1674-1682. https://doi.org/10.1021/jf405003u
Loncaric, A., Kopjar, M., & Piližota, V. (2017). Improving the quality of apple purée. Journal of Food Science and Technology, 54(10), 3201-3207. https://doi.org/10.1007/s13197-017-2760-z
Loncaric, A., Pichler, A., Trtinjak, I., Pilizota, V., & Kopjar, M. (2016). Phenolics and antioxidant activity of freeze-dried sour cherry puree with addition of disaccharides. LWT - Food Science and Technology, 73, 391-396. https://doi.org/10.1016/j.lwt.2016.06.040
Lund, M. N., & Ray, C. A. (2017). Control of Maillard reactions in foods: Strategies and chemical mechanisms. Journal of Agricultural and Food Chemistry, 65(23), 4537-4552. https://doi.org/10.1021/acs.jafc.7b00882
Luyckx, J., & Baudouin, C. (2011). Trehalose: An intriguing disaccharide with potential for medical application in ophthalmology. Clinical Ophthalmology, 5(1), 577-581. https://doi.org/10.2147/OPTH.S18827
Ma, L. K., Zhang, B., Deng, S. G., & Xie, C. (2015). Comparison of the cryoprotective effects of trehalose, alginate, and its oligosaccharides on peeled shrimp (litopenaeus vannamei) during frozen storage. Journal of Food Science, 80(3), C540-C546. https://doi.org/10.1111/1750-3841.12793
Mancini, R. J., Lee, J., & Maynard, H. D. (2012). Trehalose glycopolymers for stabilization of protein conjugates to environmental stressors. Journal of the American Chemical Society, 134(20), 8474-8479. https://doi.org/10.1021/ja2120234
Mandal, S., Debnath, K., Jana, N. R., & Jana, N. R. (2017). Trehalose-functionalized gold nanoparticle for inhibiting intracellular protein aggregation. Langmuir, 33(49), 13996-14003. https://doi.org/10.1021/acs.langmuir.7b02202
Maréchal, L. R., & Belocopitow, E. (1972). Metabolism of trehalose in Euglena gracilis. I. Partial purification and some properties of trehalose phosphorylase. Journal of Biological Chemistry, 247(10), 3223-3228. https://doi.org/10.1016/S0021-9258(19)45234-4
Martin, J. S. H., Monaghan, T. M., & Wilcox, M. H. (2016). Clostridium difficile infection: Epidemiology, diagnosis and understanding transmission. Nature Reviews Gastroenterology and Hepatology, 13(4), 206-216. https://doi.org/10.1038/nrgastro.2016.25
Maruta, K., Hattori, K., Nakada, T., Kubota, M., Sugimoto, T., & Kurimoto, M. (1996). Cloning and sequencing of trehalose biosynthesis genes from rhizobium sp. M-ll. Bioscience, Biotechnology and Biochemistry, 60(4), 717-720. https://doi.org/10.1271/bbb.60.717
Maruta, K., Mitsuzumi, H., Nakada, T., Kubota, M., Chaen, H., Fukuda, S., Sugimoto, T., & Kurimoto, M. (1996). Cloning and sequencing of a cluster of genes encoding novel enzymes of trehalose biosynthesis from thermophilic archaebacterium Sulfolobus acidocaldarius. Biochimica et Biophysica Acta - General Subjects, 1291(3). https://doi.org/10.1016/S0304-4165(96)00082-7
Moriano, M. E., & Alamprese, C. (2017). Honey, trehalose and erythritol as sucrose-alternative sweeteners for artisanal ice cream. A pilot study. LWT - Food Science and Technology, 75, 329-344. https://doi.org/10.1016/j.lwt.2016.08.057
Murphy, H. N., Stewart, G. R., Mischenko, V. v., Apt, A. S., Harris, R., McAlister, M. S. B., Driscoll, P. C., Young, D. B., & Robertson, B. D. (2005). The OtsAB pathway is essential for trehalose biosynthesis in Mycobacterium tuberculosis. Journal of Biological Chemistry, 280(15), 14524-14529. https://doi.org/10.1074/jbc.M414232200
Murphy, T. A., & Wyatt, G. R. (1965). The enzymes of glycogen and trehalose synthesis in silk moth fat body. The Journal of Biological Chemistry, 240, 1500-1508. https://doi.org/10.1016/s0021-9258(18)97463-6
Murray, B. S., & Liang, H. J. (1999). Enhancement of the foaming properties of protein dried in the presence of trehalose. Journal of Agricultural and Food Chemistry, 47(12), 4984-4991. https://doi.org/10.1021/jf990206n
Murray, I. A., Coupland, K., Smith, J. A., Ansell, I. D., & Long, R. G. (2000). Intestinal trehalase activity in a UK population: Establishing a normal range and the effect of disease. British Journal of Nutrition, 83(3), 241-245. https://doi.org/10.1017/S0007114500000313
Nakada, T., Ikegami, S., Chaen, H., Kubota, M., Fukuda, S., Sugimoto, T., Kurimoto, M., & Tsujisaka, O. (1996). Purification and characterization of thermostable maltooligosyl trehalose trehalohydrolase from the thermoacidophilic archaebacterium sulfolobus acidocaldarius. Bioscience, Biotechnology and Biochemistry, 60(2), 267-270. https://doi.org/10.1271/bbb.60.263
Nakada, T., Maruta, K., Tsusaki, K., Kubota, M., Chaen, H., Sugimoto, T., Kurimoto, M., & Tsujisaka, Y. (1995). Purification and properties of a novel enzyme, maltooligosyl trehalose synthase, from Arthrobactersp. Q36. Bioscience, Biotechnology, and Biochemistry, 59(12), 2210-2214. https://doi.org/10.1271/bbb.59.2210
Nie, S. P., Huang, J. G., Hu, J. L., Zhang, Y. N., Wang, S., Li, C., Marcone, M., & Xie, M. Y. (2013). Effect of pH, temperature and heating time on the formation of furan in sugar-glycine model systems. Food Science and Human Wellness, 2(2), 87-92. https://doi.org/10.1016/j.fshw.2013.05.001
Nishimoto, T., Nakada, T., Chaen, H., Fukuda, S., Sugimoto, T., Kurimoto, M., & Tsujisaka, Y. (1996). Purification and characterization of a thermostable trehalose synthase from Thermus aquaticus. Bioscience, Biotechnology and Biochemistry, 60(5), 835-839. https://doi.org/10.1271/bbb.60.835
Nishimoto, T., Nakano, M., Nakada, T., Chaen, H., Fukuda, S., Sugimoto, T., Kurimoto, M., & Tsujisaka, Y. (1996). Purification and properties of a novel enzyme, trehalose synthase, from Pimelobacter sp. R48. Bioscience, Biotechnology and Biochemistry, 60(4), 640-644. https://doi.org/10.1271/bbb.60.640
Nishizaki, Y., Yoshizane, C., Toshimori, Y., Arai, N., Akamatsu, S., Hanaya, T., Arai, S., Ikeda, M., & Kurimoto, M. (2000). Disaccharide-trehalose inhibits bone resorption in ovarieciomized mice. Nutrition Research, 20(5), 653-664. https://doi.org/10.1016/S0271-5317(00)00155-X
Nooshkam, M., Varidi, M., & Bashash, M. (2019). The Maillard reaction products as food-born antioxidant and antibrowning agents in model and real food systems. Food Chemistry, 275, 644-660. https://doi.org/10.1016/j.foodchem.2018.09.083
Nwaka, S., & Holzer, H. (1997). Molecular biology of trehalose and the trehalases in the yeast Saccharomyces cerevisiae. Progress in Nucleic Acid Research and Molecular Biology, 58(C), 197-237. https://doi.org/10.1016/S0079-6603(08)60037-9
Ohtake, S., & Wang, Y. J. (2011). Trehalose: Current use and future applications. Journal of Pharmaceutical Sciences, 100(6), 2020-2053. https://doi.org/10.1002/jps.22458
Oku, K., Chaen, H., Fukuda, S., & Kurimoto, M. (1999). Effect of trehalose on suppression of trimethylamine - formation from boiling fish meat. Nippon Shokuhin Kagaku Kogaku Kaishi, 46(5), 319-322. https://doi.org/10.3136/nskkk.46.319
Oku, K., Kurose, M., Chaen, H., Fukuda, S., Tsujisaka, Y., & Sakurai, Mi. (2005). Suppressive effect of trehalose on radical oxidation of unsaturated fatty acids. Journal of Applied Glycoscience, 52(4), 381-385. https://doi.org/10.5458/jag.52.381
Oku, K., Kurose, M., Kubota, M., Fukuda, S., Kurimoto, M., Tsujisaka, Y., & Sakurai, M. (2003). Inhibitory effect of trehalose on the autoxidation of unsaturated fatty acids by water/ethanol system. Nippon Shokuhin Kagaku Kogaku Kaishi, 50(3), 133-137. https://doi.org/10.3136/nskkk.50.133
Oku, K., Kurose, M., Ogawa, T., Kubota, M., Chaen, H., Fukuda, S., & Tsujisaka, Y. (2005). Suppressive effect of trehalose on acrylamide formation from asparagine and reducing saccharides. Bioscience, Biotechnology and Biochemistry, 69(8), 1520-1526. https://doi.org/10.1271/bbb.69.1520
Oku, K., Sawatani, I., Chaen, H., Fukuda, S., & Kurimoto, M. (1998). Trehalose content in foods. Nippon Shokuhin Kagaku Kogaku Kaishi, 45(6), 381-384. https://doi.org/10.3136/nskkk.45.381
Oku, K., Sawatani, I., Sugimoto, S., Kanbe, M., Takeuchi, K., Murai, S., Kurose, M., Kubota, M., & Fukuda, S. (2002). Functional properties of trehalose. Journal of Applied Glycoscience, 49(3), 351-357.
Oku, T., & Okazaki, M. (1998). Transitory laxative threshold of trehalose and lactulose in healthy women. Journal of Nutritional Science and Vitaminology, 44(6), 787-798. https://doi.org/10.3177/jnsv.44.787
Olgenblum, G. I., Sapir, L., & Harries, D. (2020). Properties of aqueous trehalose mixtures: Glass transition and hydrogen bonding. Journal of Chemical Theory and Computation, 16(2), 1249-1262. https://doi.org/10.1021/acs.jctc.9b01071
Olsson, C., Zangana, R., & Swenson, J. (2020). Stabilization of proteins embedded in sugars and water as studied by dielectric spectroscopy. Physical Chemistry Chemical Physics, 22(37), 21197-21207. https://doi.org/10.1039/d0cp03281f
O'Neill, M. K., Piligian, B. F., Olson, C. D., Woodruff, P. J., & Swarts, B. M. (2017). Tailoring trehalose for biomedical and biotechnological applications. Pure and Applied Chemistry, 89(9), 1223-1249. https://doi.org/10.1515/pac-2016-1025
Osako, K., Hossain, M. A., Kuwahara, K., & Nozaki, Y. (2005). Effect of trehalose on the gel-forming ability, state of water and myofibril denaturation of horse mackerel Trachurus japonicus surimi during frozen storage. Fisheries Science, 71(2), 367-373. https://doi.org/10.1111/j.1444-2906.2005.00973.x
Paiva, C. L. A., & Panek, A. D. (1996). Biotechnological applications of the disaccharide trehalose. Biotechnology Annual Review, 2, 293-314. https://doi.org/10.1016/S1387-2656(08)70015-2
Pan, J., Shen, H., & Luo, Y. (2010). Cryoprotective effects of trehalose on grass carp (ctenopharyngodon idellus) surimi during frozen storage. Journal of Food Processing and Preservation, 34(4), 715-727. https://doi.org/10.1111/j.1745-4549.2009.00388.x
Panek, A. D. (1995). Trehalose metabolism-new horizons in technological applications. Brazilian Journal of Medical and Biological Research, 28(2), 169-181.
Panescu, P. H., Ko, J. H., & Maynard, H. D. (2019). Scalable trehalose-functionalized hydrogel synthesis for high-temperature protection of enzymes. Macromolecular Materials and Engineering, 304(6), 1800782. https://doi.org/10.1002/mame.201800782
Parascandola, P., de Alteriis, E., & Scardi, V. (1993). Invertase and acid phosphatase in free and gel-immobilized cells of Saccharomyces cerevisiae grown under different cultural conditions. Enzyme and Microbial Technology, 15(1), 42-49. https://doi.org/10.1016/0141-0229(93)90114-H
Patist, A., & Zoerb, H. (2005). Preservation mechanisms of trehalose in food and biosystems. Colloids and Surfaces B: Biointerfaces, 40(2), 107-113. https://doi.org/10.1016/j.colsurfb.2004.05.003
Peng, B., Li, Y., Ding, S., & Yang, J. (2017). Characterization of textural, rheological, thermal, microstructural, and water mobility in wheat flour dough and bread affected by trehalose. Food Chemistry, 233, 369-377. https://doi.org/10.1016/j.foodchem.2017.04.108
Penkov, S., Mende, F., Zagoriy, V., Erkut, C., Martin, R., Pässler, U., Schuhmann, K., Schwudke, D., Gruner, M., Reichert-Müller, T., Shevchenko, A., Knölker, H. J., & Kurzchalia, T. (2010). Maradolipids: Diacyltrehalose glycolipids specific to dauer larva in Caenorhabditis elegans. Angewandte Chemie - International Edition, 49(49), 9430-9435. https://doi.org/10.1002/anie.201004466
Pereira, M. D., Eleutherio, E. C. A., & Panek, A. D. (2001). Acquisition of tolerance against oxidative damage in Saccharomyces cerevisiae. BMC Microbiology, 1, 11. https://doi.org/10.1186/1471-2180-1-11
Pérez, L. M., Piccirilli, G. N., Delorenzi, N. J., & Verdini, R. A. (2016). Effect of different combinations of glycerol and/or trehalose on physical and structural properties of whey protein concentrate-based edible films. Food Hydrocolloids, 56, 352-359. https://doi.org/10.1016/j.foodhyd.2015.12.037
Perfect, J. R., Tenor, J. L., Miao, Y., & Brennan, R. G. (2017). Trehalose pathway as an antifungal target. Virulence, 8(2), 143-149. https://doi.org/10.1080/21505594.2016.1195529
Petzold, E. W., Himmelreich, U., Mylonakis, E., Rude, T., Toffaletti, D., Cox, G. M., Miller, J. L., & Perfect, J. R. (2006). Characterization and regulation of the trehalose synthesis pathway and its importance in the pathogenicity of Cryptococcus neoformans. Infection and Immunity, 74(10), 5877-5887. https://doi.org/10.1128/IAI.00624-06
Phoon, P. Y., Galindo, F. G., Vicente, A., & Dejmek, P. (2008). Pulsed electric field in combination with vacuum impregnation with trehalose improves the freezing tolerance of spinach leaves. Journal of Food Engineering, 88(1), 144-148. https://doi.org/10.1016/j.jfoodeng.2007.12.016
Pilon-Smits, E. A. H., Terry, N., Sears, T., Kim, H., Zayed, A., Hwang, S., van Dun, K., Voogd, E., Verwoerd, T. C., Krutwagen, R. W. H. H., & Goddijn, O. J. M. (1998). Trehalose-producing transgenic tobacco plants show improved growth performance under drought stress. Journal of Plant Physiology, 152(4-5), 525-532. https://doi.org/10.1016/S0176-1617(98)80273-3
Ploypetchara, T., & Gohtani, S. (2020). Change in characteristics of film based on rice starch blended with sucrose, maltose, and trehalose after storage. Journal of Food Science, 85(5), 1470-1478. https://doi.org/10.1111/1750-3841.15021
Portbury, S. D., Hare, D. J., Finkelstein, D. I., & Adlard, P. A. (2017). Trehalose improves traumatic brain injury-induced cognitive impairment. PLoS ONE, 12(8), e0183683. https://doi.org/10.1371/journal.pone.0183683
Portmann, M. -O, & Birch, G. (1995). Sweet taste and solution properties of α,α-trehalose. Journal of the Science of Food and Agriculture, 69(3), 275-281. https://doi.org/10.1002/jsfa.2740690303
Prestrelski, S. J., Tedeschi, N., Arakawa, T., & Carpenter, J. F. (1993). Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers. Biophysical Journal, 65(2), 661-671. https://doi.org/10.1016/S0006-3495(93)81120-2
Qu, Q., Lee, S. J., & Boos, W. (2004). TreT, a novel trehalose glycosyltransferring synthase of the hyperthermophilic archaeon Thermococcus litoralis. Journal of Biological Chemistry, 279(46), 47890-47897. https://doi.org/10.1074/jbc.M404955200
Reid, D. S., & Levine, H. (1991). Beyond water activity: Recent advances based on an alternative approach to the assessment of food quality and safety. Critical Reviews in Food Science and Nutrition, 30(2-3), 115-360. https://doi.org/10.1080/10408399109527543
Reis, J., Sitaula, R., & Bhowmick, S. (2009). Water activity and glass transition temperatures of disaccharide based buffers for desiccation preservation of biologics. Journal of Biomedical Science and Engineering, 02(08), 594-605. https://doi.org/10.4236/jbise.2009.28086
Richards, A. B., & Dexter, L. B. (2016). Trehalose. In (L. O. B. Nabors Ed.), Alternative Sweeteners: Fourth Edition (4th ed.). CRC Press.
Richards, A. B., Krakowka, S., Dexter, L. B., Schmid, H., Wolterbeek, A. P. M., Waalkens-Berendsen, D. H., Shigoyuki, A., & Kurimoto, M. (2002). Trehalose: A review of properties, history of use and human tolerance, and results of multiple safety studies. Food and Chemical Toxicology, 40(7), 871-898. https://doi.org/10.1016/S0278-6915(02)00011-X
Rodríguez-Lucena, D., Benito, J. M., Álvarez, E., Jaime, C., Perez-Miron, J., Mellet, C. O., & García Fernández, J. M. (2008). Synthesis, structure, and inclusion capabilities of trehalose-based cyclodextrin analogues (cyclotrehalans). Journal of Organic Chemistry, 73(8), 2967-2979. https://doi.org/10.1021/jo800048s
Roser, B. (1991). Trehalose, a new approach to premium dried foods. Trends in Food Science and Technology, 2(C), 166-169. https://doi.org/10.1016/0924-2244(91)90671-5
Roth, R., & Sussman, M. (1966). Trehalose synthesis in the cellular slime mold Dictyostelium discoideum. BBA - Enzymology and Biological Oxidation, 122(2), 225-231. https://doi.org/10.1016/0926-6593(66)90064-6
Rousseau, P., Halvorson, H. O., Bulla, L. A., & St Julian, G. (1972). Germination and outgrowth of single spores of Saccharomyces cerevisiae viewed by scanning electron and phase-contrast microscopy. Journal of Bacteriology, 109(3), 1232-1238. https://doi.org/10.1128/jb.109.3.1232-1238.1972
Ryll, R., Kumazawa, Y., & Yano, I. (2001). Immunological properties of trehalose dimycolate (cord factor) and other mycolic acid-containing glycolipids - A review. Microbiology and Immunology, 45(12), 801-811. https://doi.org/10.1111/j.1348-0421.2001.tb01319.x
Ryu, S. I., Park, C. S., Cha, J., Woo, E. J., & Lee, S. B. (2005). A novel trehalose-synthesizing glycosyltransferase from Pyrococcus horikoshii: Molecular cloning and characterization. Biochemical and Biophysical Research Communications, 329(2), 429-436. https://doi.org/10.1016/j.bbrc.2005.01.149
Saito, K., Yamazaki, H., Ohnishi, Y., Fujimoto, S., Takahashi, E., & Horinouchi, S. (1998). Production of trehalose synthase from a basidiomycete, Grifola frondosa, in Escherichia coli. Applied Microbiology and Biotechnology, 50(2), 193-198. https://doi.org/10.1007/s002530051276
Saleheen, D., Natarajan, P., Armean, I. M., Zhao, W., Rasheed, A., Khetarpal, S. A., Won, H. H., Karczewski, K. J., O'Donnell-Luria, A. H., Samocha, K. E., Weisburd, B., Gupta, N., Zaidi, M., Samuel, M., Imran, A., Abbas, S., Majeed, F., Ishaq, M., Akhtar, S., … Kathiresan, S. (2017). Human knockouts and phenotypic analysis in a cohort with a high rate of consanguinity. Nature, 544(7649), 235-239. https://doi.org/10.1038/nature22034
Saleki-Gerhardt, A., & Zografi, G. (1994). Non-isothermal and isothermal crystallization of sucrose from the amorphous state. Pharmaceutical Research: An Official Journal of the American Association of Pharmaceutical Scientists, 11(8), 1166-1173. https://doi.org/10.1023/A:1018945117471
Santos, H., & da Costa, M. S. (2002). Compatible solutes of organisms that live in hot saline environments. Environmental Microbiology, 4(9), 501-509. https://doi.org/10.1046/j.1462-2920.2002.00335.x
Sarkar, S., Davies, J. E., Huang, Z., Tunnacliffe, A., & Rubinsztein, D. C. (2007). Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and α-synuclein. Journal of Biological Chemistry, 282(8), 5641-5652. https://doi.org/10.1074/jbc.M609532200
Sasano, Y., Haitani, Y., Hashida, K., Ohtsu, I., Shima, J., & Takagi, H. (2012). Simultaneous accumulation of proline and trehalose in industrial baker's yeast enhances fermentation ability in frozen dough. Journal of Bioscience and Bioengineering, 113(5), 592-595. https://doi.org/10.1016/j.jbiosc.2011.12.018
Saund, K., Rao, K., Young, V. B., & Snitkin, E. S. (2020). Genetic determinants of trehalose utilization are not associated with severe Clostridium difficile infection outcome. Open Forum Infectious Diseases, 7(1), ofz548. https://doi.org/10.1093/ofid/ofz548
Schebor, C., Burin, L., Buera, M. D. P., & Chirife, J. (1999). Stability to hydrolysis and browning of trehalose, sucrose and raffinose in low-moisture systems in relation to their use as protectants of dry biomaterials. LWT - Food Science and Technology, 32(8), 481-485. https://doi.org/10.1006/fstl.1999.0576
Schiraldi, C., di Lernia, I., & de Rosa, M. (2002). Trehalose production: Exploiting novel approaches. Trends in Biotechnology, 20(10), 420-425. https://doi.org/10.1016/S0167-7799(02)02041-3
Schwenk, M. (2016). Investigating the loss of crystal structure in carbohydrate materials [Ph.D. dissertation]. University of Illinois at Urbana-Champaign.
Sei, T., Gonda, T., & Arima, Y. (2002). Growth rate and morphology of ice crystals growing in a solution of trehalose and water. Journal of Crystal Growth, 240(1-2), 218-229. https://doi.org/10.1016/S0022-0248(02)00875-8
Shi, L., Sutter, B. M., Ye, X., & Tu, B. P. (2010). Trehalose is a key determinant of the quiescent metabolic state that fuels cell cycle progression upon return to growth. Molecular Biology of the Cell, 21(12), 1982-1990. https://doi.org/10.1091/mbc.E10-01-0056
Shukla, E., Thorat, L. J., Nath, B. B., & Gaikwad, S. M. (2015). Insect trehalase: Physiological significance and potential applications. Glycobiology, 25(4), 357-367. https://doi.org/10.1093/glycob/cwu125
Silljé, H. H. W., Paalman, J. W. G., ter Schure, E. G., Olsthoorn, S. Q. B., Verkleij, A. J., Boonstra, J., & Verrips, C. T. (1999). Function of trehalose and glycogen in cell cycle progression and cell viability in Saccharomyces cerevisiae. Journal of Bacteriology, 181(2), 396-400. https://doi.org/10.1128/jb.181.2.396-400.1999
Singer, M. A., & Lindquist, S. (1998a). Multiple effects of trehalose on protein folding in vitro and in vivo. Molecular Cell, 1(5), 639-648. https://doi.org/10.1016/S1097-2765(00)80064-7
Singer, M. A., & Lindquist, S. (1998b). Thermotolerance in Saccharomyces cerevisiae: The Yin and Yang of trehalose. Trends in Biotechnology, 16(11), 460-468. https://doi.org/10.1016/S0167-7799(98)01251-7
Sokołowska, E., Sadowska, A., Sawicka, D., Kotulska-Bąblińska, I., & Car, H. (2021). A head-to-head comparison review of biological and toxicological studies of isomaltulose, d-tagatose, and trehalose on glycemic control. Critical Reviews in Food Science and Nutrition, 62(21), 5679-5704. https://doi.org/10.1080/10408398.2021.1895057
Sola-Penna, M., & Meyer-Fernandes, J. R. (1998). Stabilization against thermal inactivation promoted by sugars on enzyme structure and function: Why is trehalose more effective than other sugars? Archives of Biochemistry and Biophysics, 360(1), 10-14. https://doi.org/10.1006/abbi.1998.0906
Song, X. S., Li, H. P., Zhang, J. B., Song, B., Huang, T., Du, X. M., Gong, A. D., Liu, Y. K., Feng, Y. N., Agboola, R. S., & Liao, Y. C. (2014). Trehalose 6-phosphate phosphatase is required for development, virulence and mycotoxin biosynthesis apart from trehalose biosynthesis in Fusarium graminearum. Fungal Genetics and Biology, 63, 24-41. https://doi.org/10.1016/j.fgb.2013.11.005
Song, X., Tang, S., Jiang, L., Zhu, L., & Huang, H. (2016). Integrated biocatalytic process for trehalose production and separation from maltose. Industrial and Engineering Chemistry Research, 55(40), 10566-10575. https://doi.org/10.1021/acs.iecr.6b02276
Sosa, N., Schebor, C., & Pérez, O. E. (2014). Encapsulation of citral in formulations containing sucrose or trehalose: Emulsions properties and stability. Food and Bioproducts Processing, 92(3), 266-274. https://doi.org/10.1016/j.fbp.2013.08.001
Sosa, N., Zamora, M. C., Chirife, J., & Schebor, C. (2011). Spray-drying encapsulation of citral in sucrose or trehalose matrices: Physicochemical and sensory characteristics. International Journal of Food Science and Technology, 46(10), 2096-2102. https://doi.org/10.1111/j.1365-2621.2011.02721.x
Sosa, N., Zamora, M. C., van Baren, C., & Schebor, C. (2014). New insights in the use of trehalose and modified starches for the encapsulation of orange essential oil. Food and Bioprocess Technology, 7(6), 1745-1755. https://doi.org/10.1007/s11947-013-1174-9
Stefanello, R. F., Machado, A. A. R., Pasqualin Cavalheiro, C., Bartholomei Santos, M. L., Nabeshima, E. H., Copetti, M. V., & Fries, L. L. M. (2018). Trehalose as a cryoprotectant in freeze-dried wheat sourdough production. LWT - Food Science and Technology, 89, 510-517. https://doi.org/10.1016/j.lwt.2017.11.011
Stick, R., & Spencer, W. (2009). Disaccharides, oligosaccharides and polysaccharides. In Carbohydrates: The Essential Molecules of Life (Second, pp. 321-314). Elsevier Science. https://doi.org/10.1016/b978-012670960-5/50011-x
Storhaug, C. L., Fosse, S. K., & Fadnes, L. T. (2017). Country, regional, and global estimates for lactose malabsorption in adults: A systematic review and meta-analysis. The Lancet Gastroenterology and Hepatology, 2(10), 738-746. https://doi.org/10.1016/S2468-1253(17)30154-1
Streeter, J. G., & Bhagwat, A. (1999). Biosynthesis of trehalose from maltooligosaccharides in Rhizobia. Canadian Journal of Microbiology, 45(8), 716-721. https://doi.org/10.1139/w99-050
Strom, A. R., & Kaasen, I. (1993). Trehalose metabolism in Escherichia coli: Stress protection and stress regulation of gene expression. Molecular Microbiology, 8(2), 205-210. https://doi.org/10.1111/j.1365-2958.1993.tb01564.x
Sun, Y., Zhu, L., Wu, T., Cai, T., Gunn, E. M., & Yu, L. (2012). Stability of amorphous pharmaceutical solids: Crystal growth mechanisms and effect of polymer additives. AAPS Journal, 14(3), 380-388. https://doi.org/10.1208/s12248-012-9345-6
Sundaramurthi, P., & Suryanarayanan, R. (2010). Trehalose crystallization during freeze-drying: Implications on lyoprotection. Journal of Physical Chemistry Letters, 1(2), 510-514. https://doi.org/10.1021/jz900338m
Sussich, F., Urbani, R., Princivalle, F., & Cesàro, A. (1998). Polymorphic amorphous and crystalline forms of trehalose. Journal of the American Chemical Society, 120(31), 7893-7899. https://doi.org/10.1021/ja9800479
Sze-Yin, S., & Lai-Hoong, C. (2013). Effects of maltodextrin and trehalose on the physical properties of chinese steamed bread made from frozen doughs. International Food Research Journal, 20(4), 1529-1535.
Tan, M., Mei, J., & Xie, J. (2021). The formation and control of ice crystal and its impact on the quality of frozen aquatic products: A review. Crystals, 11(1), 68. https://doi.org/10.3390/cryst11010068
Tanaka, K. (2009). Develompent of Treha(R) and its properties. Food Industry, 52(10), 45-51.
Tapia, H., Young, L., Fox, D., Bertozzi, C. R., & Koshland, D. (2015). Increasing intracellular trehalose is sufficient to confer desiccation tolerance to Saccharomyces cerevisiae. Proceedings of the National Academy of Sciences of the United States of America, 112(19), 6122-6127. https://doi.org/10.1073/pnas.1506415112
Thammahong, A., Puttikamonkul, S., Perfect, J. R., Brennan, R. G., & Cramer, R. A. (2017). Central role of the trehalose biosynthesis pathway in the pathogenesis of human fungal infections: Opportunities and challenges for therapeutic development. Microbiology and Molecular Biology Reviews, 81(2), e00053-16. https://doi.org/10.1128/mmbr.00053-16
Thevelein, J. M. (1984). Regulation of trehalose mobilization in fungi. Microbiological Reviews, 48(1), 42-59. https://doi.org/10.1128/mmbr.48.1.42-59.1984
Tonnis, W. F., Mensink, M. A., de Jager, A., van der Voort Maarschalk, K., Frijlink, H. W., & Hinrichs, W. L. J. (2015). Size and molecular flexibility of sugars determine the storage stability of freeze-dried proteins. Molecular Pharmaceutics, 12(3), 684-694. https://doi.org/10.1021/mp500423z
Tournu, H., Fiori, A., & van Dijck, P. (2013). Relevance of trehalose in pathogenicity: Some general rules, yet many exceptions. PLoS Pathogens, 9(8), e1003447. https://doi.org/10.1371/journal.ppat.1003447
Trevelyan, W. E., & Harrison, J. S. (1956). Studies on yeast metabolism. 5. The trehalose content of baker's yeast during anaerobic fermentation. The Biochemical Journal, 62(2), 177-183. https://doi.org/10.1042/bj0620177b
Tsusaki, K., Nishimoto, T., Nakada, T., Kubota, M., Chaen, H., Sugimoto, T., & Kurimoto, M. (1996). Cloning and sequencing of trehalose synthase gene from Pimelobacter sp. R48. Biochimica et Biophysica Acta - General Subjects, 1290(1), 1-3. https://doi.org/10.1016/0304-4165(96)00023-2
Tvorogova, A. A., Landikhovskaya, A. v., Kazakova, N. v., Zakirova, R. R., & Pivtsaeva, M. M. (2021). Scientific and practical aspects of trehalose contain in ice cream without sucrose. IOP Conference Series: Earth and Environmental Science, 640(5), 052017. https://doi.org/10.1088/1755-1315/640/5/052017
Vanaporn, M., & Titball, R. W. (2020). Trehalose and bacterial virulence. Virulence, 11(1), 1192-1202. https://doi.org/10.1080/21505594.2020.1809326
Walmagh, M., Zhao, R., & Desmet, T. (2015). Trehalose analogues: Latest insights in properties and biocatalytic production. International Journal of Molecular Sciences, 16(6), 13729-13745. https://doi.org/10.3390/ijms160613729
Wang, J., Ren, X., Wang, R., Su, J., & Wang, F. (2017). Structural characteristics and function of a new kind of trehalose synthase from Thermobaculum terrenum. Journal of Agricultural and Food Chemistry, 65(35), 7726-7735. https://doi.org/10.1021/acs.jafc.7b02732
Wang, S., Li, C., Copeland, L., Niu, Q., & Wang, S. (2015). Starch retrogradation: A comprehensive review. Comprehensive Reviews in Food Science and Food Safety, 14(5), 568-585. https://doi.org/10.1111/1541-4337.12143
Wang, Z., Qi, J., & Goddard, J. M. (2021). Concentrated sugar solutions protect lactase from thermal inactivation. International Dairy Journal, 123, 105168. https://doi.org/10.1016/j.idairyj.2021.105168
Wannet, W. J. B., Op Den Camp, H. J. M., Wisselink, H. W., van der Drift, C., van Griensven, L. J. L. D., & Vogels, G. D. (1998). Purification and characterization of trehalose phosphorylase from the commercial mushroom Agaricus bisporus. Biochimica et Biophysica Acta - General Subjects, 1425(1), 177-188. https://doi.org/10.1016/S0304-4165(98)00066-X
Weihrauch, J. L., & Son, Y. S. (1983). Phospholipid content of foods. Journal of the American Oil Chemists’ Society, 60(12), 1971-1978. https://doi.org/10.1007/BF02669968
Wharton, D. A., Judge, K. F., & Worland, M. R. (2000). Cold acclimation and cryoprotectants in a freeze-tolerant Antarctic nematode, Panagrolaimus davidi. Journal of Comparative Physiology - B Biochemical, Systemic, and Environmental Physiology, 170(4), 321-327. https://doi.org/10.1007/s003600000106
Whelan, A. P., Regand, A., Vega, C., Kerry, J. P., & Goff, H. D. (2008). Effect of trehalose on the glass transition and ice crystal growth in ice cream. International Journal of Food Science and Technology, 43(3), 510-516. https://doi.org/10.1111/j.1365-2621.2006.01484.x
Wiggers, H. A. L. (1832). Untersuchung über das Mutterkorn, Secale cornutum. Annalen Der Pharmacie, 1(2), 129-182. https://doi.org/10.1002/jlac.18320010202
Wilson, R. A., Jenkinson, J. M., Gibson, R. P., Littlechild, J. A., Wang, Z. Y., & Talbot, N. J. (2007). Tps1 regulates the pentose phosphate pathway, nitrogen metabolism and fungal virulence. EMBO Journal, 26(15), 3673-3685. https://doi.org/10.1038/sj.emboj.7601795
Wolf, A., Krämer, R., & Morbach, S. (2003). Three pathways for trehalose metabolism in Corynebacterium glutamicum ATCC13032 and their significance in response to osmotic stress. Molecular Microbiology, 49(4), 1119-1134. https://doi.org/10.1046/j.1365-2958.2003.03625.x
Wu, S. (2016). Effect of trehalose on the state of water, protein denaturation and gel-forming ability of weever surimi. International Journal of Food Properties, 19(3), 521-525. https://doi.org/10.1080/10942912.2015.1033550
Wu, S., Pan, S., & Wang, H. (2014). Effect of trehalose on Lateolabrax japonicus myofibrillar protein during frozen storage. Food Chemistry, 160, 281-285. https://doi.org/10.1016/j.foodchem.2014.03.100
Wyatt, G. R., & Kale, G. F. (1957). The chemistry of insect hemolymph. II. Trehalose and other carbohydrates. The Journal of General Physiology, 40(6), 833-847. https://doi.org/10.1085/jgp.40.6.833
Xie, G., & Timasheff, S. N. (1997). The thermodynamic mechanism of protein stabilization by trehalose. Biophysical Chemistry, 64(1-3), 25-43. https://doi.org/10.1016/S0301-4622(96)02222-3
Xu, C., Li, X., Wang, F., Weng, H., & Yang, P. (2013). Trehalose prevents neural tube defects by correcting maternal diabetes-suppressed autophagy and neurogenesis. American Journal of Physiology - Endocrinology and Metabolism, 305(5), E667-E678. https://doi.org/10.1152/ajpendo.00185.2013
Yamamoto, T., Maruta, K., Watanabe, H., Yamashita, H., Kubota, M., Fukuda, S., & Kurimoto, M. (2001). Trehalose-producing operon treYZ from Arthrobacter ramosus S34. Bioscience, Biotechnology and Biochemistry, 65(6), 1419-1423. https://doi.org/10.1271/bbb.65.1419
Yaribeygi, H., Yaribeygi, A., Sathyapalan, T., & Sahebkar, A. (2019). Molecular mechanisms of trehalose in modulating glucose homeostasis in diabetes. Diabetes and Metabolic Syndrome: Clinical Research and Reviews, 13(3), 2214-2218. https://doi.org/10.1016/j.dsx.2019.05.023
Zaragoza, O., Blazquez, M. A., & Gancedo, C. (1998). Disruption of the Candida albicans TPS1 gene encoding trehalose-6-phosphate synthase impairs formation of hyphae and decreases infectivity. Journal of Bacteriology, 180(15), 3809-3815. https://doi.org/10.1128/jb.180.15.3809-3815.1998
Zhang, B., Cao, H., Lin, H., Deng, S., & Wu, H. (2019). Insights into ice-growth inhibition by trehalose and alginate oligosaccharides in peeled Pacific white shrimp (Litopenaeus vannamei) during frozen storage. Food Chemistry, 278, 482-490. https://doi.org/10.1016/j.foodchem.2018.11.087
Zhang, B., Wu, H., Yang, H., Xiang, X., Li, H., & Deng, S. (2017). Cryoprotective roles of trehalose and alginate oligosaccharides during frozen storage of peeled shrimp (Litopenaeus vannamei). Food Chemistry, 228, 257-264. https://doi.org/10.1016/j.foodchem.2017.01.124
Zhang, R., Pan, Y. T., He, S., Lam, M., Brayer, G. D., Elbein, A. D., & Withers, S. G. (2011). Mechanistic analysis of trehalose synthase from Mycobacterium smegmatis. Journal of Biological Chemistry, 286(41), 35601-35609. https://doi.org/10.1074/jbc.M111.280362
Zhang, X., Tong, Q. Y., & Ren, F. (2012). Influence of glucose, sucrose and trehalose on the freeze-thaw stability of tapioca starch gels. Advance Journal of Food Science and Technology, 4(4), 225-230.
Zhang, Y., & Debosch, B. J. (2019). Using trehalose to prevent and treat metabolic function: Effectiveness and mechanisms. Current Opinion in Clinical Nutrition and Metabolic Care, 22(4), 303-310. https://doi.org/10.1097/MCO.0000000000000568
Zhou, A., Benjakul, S., Pan, K., Gong, J., & Liu, X. (2006). Cryoprotective effects of trehalose and sodium lactate on tilapia (Sarotherodon nilotica) surimi during frozen storage. Food Chemistry, 96(1), 96-103. https://doi.org/10.1016/j.foodchem.2005.02.013
Zhou, J., Peng, Y., & Xu, N. (2007). Effect of trehalose on fresh bread and bread staling. Cereal Foods World, 52(6), 313-316. https://doi.org/10.1094/CFW-52-6-0313
Zhu, P., Yang, Y., Zou, L., Gao, J., Wang, B., Bian, X., Yu, D., Liu, L., Lin, C., & Zhang, N. (2021). The effect of trehalose on the thermodynamic stability and emulsification of soybean 11S globulin in the molten globule state. Food Hydrocolloids, 118, 106811. https://doi.org/10.1016/j.foodhyd.2021.106811
Zlatić, E., Pichler, A., Lončarić, A., Vidrih, R., Požrl, T., Hribar, J., Piližota, V., & Kopjar, M. (2017). Volatile compounds of freeze-dried sour cherry puree affected by the addition of sugars. International Journal of Food Properties, 20(sup1), S449-S456. https://doi.org/10.1080/10942912.2017.1299175