Preparation of combined cross-linked enzyme aggregates containing galactitol dehydrogenase and NADH oxidase for L-tagatose synthesis via in situ cofactor regeneration.


Journal

Bioprocess and biosystems engineering
ISSN: 1615-7605
Titre abrégé: Bioprocess Biosyst Eng
Pays: Germany
ID NLM: 101088505

Informations de publication

Date de publication:
Feb 2022
Historique:
received: 23 09 2021
accepted: 09 11 2021
pubmed: 20 11 2021
medline: 8 4 2022
entrez: 19 11 2021
Statut: ppublish

Résumé

The combined cross-linked enzyme aggregates (combi-CLEAs) containing galactitol dehydrogenase (Gdh) and NADH oxidase (Nox) were prepared for L-tagatose synthesis. To prevent the excess consumption of cofactor, Nox in the combi-CLEAs was used to in situ regenerate NAD

Identifiants

pubmed: 34797400
doi: 10.1007/s00449-021-02665-w
pii: 10.1007/s00449-021-02665-w
doi:

Substances chimiques

Cross-Linking Reagents 0
Enzymes, Immobilized 0
Hexoses 0
Multienzyme Complexes 0
Sugar Alcohol Dehydrogenases EC 1.1.-
galactitol 2-dehydrogenase EC 1.1.1.16
NADH oxidase EC 1.6.-
NADH, NADPH Oxidoreductases EC 1.6.-
tagatose T7A20Y888Y

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

353-364

Subventions

Organisme : Natural Science Foundation of Guangxi Province
ID : 2019GXNSFAA185059

Informations de copyright

© 2021. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.

Références

Roy S, Chikkerur J, Roy SC et al (2018) Tagatose as a potential nutraceutical: production, properties, biological roles, and applications. J Food Sci 83:2699–2709. https://doi.org/10.1111/1750-3841.14358
doi: 10.1111/1750-3841.14358 pubmed: 30334250
Oh D-K (2007) Tagatose: properties, applications, and biotechnological processes. Appl Microbiol Biotechnol 76:1–8. https://doi.org/10.1007/s00253-007-0981-1
doi: 10.1007/s00253-007-0981-1 pubmed: 17492284
Roh HJ, Kim P, Park YC et al (2000) Bioconversion of D-galactose into D-tagatose by expression of L-arabinose isomerase. Biotechnol Appl Biochem 31:1–4. https://doi.org/10.1042/ba19990065
doi: 10.1042/ba19990065 pubmed: 10669396
Guerrero-Wyss M, Durán Agüero S, Angarita Dávila L (2018) D-tagatose is a promising sweetener to control glycaemia: a new functional food. BioMed Res Int 2018:1–7. https://doi.org/10.1155/2018/8718053
doi: 10.1155/2018/8718053
Espinosa I, Fogelfeld L (2010) Tagatose: from a sweetener to a new diabetic medication? Exp Opin Investig Drugs 19:285–294. https://doi.org/10.1517/13543780903501521
doi: 10.1517/13543780903501521
Patel SKS, Otari SV, Chan Kang Y, Lee J-K (2017) Protein–inorganic hybrid system for efficient his-tagged enzymes immobilization and its application in L-xylulose production. RSC Adv 7:3488–3494. https://doi.org/10.1039/C6RA24404A
doi: 10.1039/C6RA24404A
Mei W, Wang L, Zang Y et al (2016) Characterization of an L-arabinose isomerase from Bacillus coagulans NL01 and its application for D-tagatose production. BMC Biotechnol 16:55. https://doi.org/10.1186/s12896-016-0286-5
doi: 10.1186/s12896-016-0286-5 pubmed: 27363468 pmcid: 4929721
Soetedjo JNM, van de Bovenkamp HH, Deuss PJ et al (2017) Biobased furanics: kinetic studies on the acid catalyzed decomposition of 2-hydroxyacetyl furan in water using Brönsted acid catalysts. ACS Sustain Chem Eng 5:3993–4001. https://doi.org/10.1021/acssuschemeng.6b03198
doi: 10.1021/acssuschemeng.6b03198 pubmed: 28480150 pmcid: 5415339
Nath A, Verasztó B, Basak S et al (2015) Synthesis of lactose-derived nutraceuticals from dairy waste whey—a review. Food Bioprocess Technol 9:16–48. https://doi.org/10.1007/s11947-015-1572-2
doi: 10.1007/s11947-015-1572-2
Drabo P, Delidovich I (2018) Catalytic isomerization of galactose into tagatose in the presence of bases and Lewis acids. Catal Commun 107:24–28. https://doi.org/10.1016/j.catcom.2018.01.011
doi: 10.1016/j.catcom.2018.01.011
Kim P (2004) Current studies on biological tagatose production using L-arabinose isomerase: a review and future perspective. Appl Microbiol Biotechnol 65:243–249. https://doi.org/10.1007/s00253-004-1665-8
doi: 10.1007/s00253-004-1665-8 pubmed: 15248040
Kohlmeier MG, Bailey-Elkin BA, Mark BL et al (2021) Characterization of the sorbitol dehydrogenase SmoS from Sinorhizobium meliloti 1021. Acta Crystallogr Sect D 77:380–390. https://doi.org/10.1107/S2059798321001017
doi: 10.1107/S2059798321001017
Wang X, Yiu H (2016) Heterogeneous catalysis mediated cofactor NADH regeneration for enzymatic reduction. ACS Catal 6:1880–1886. https://doi.org/10.1021/acscatal.5b02820
doi: 10.1021/acscatal.5b02820
Hwang ET, Lee S (2019) Multienzymatic cascade reactions via enzyme complex by immobilization. ACS Catal 9:4402–4425. https://doi.org/10.1021/acscatal.8b04921
doi: 10.1021/acscatal.8b04921
Wang X, Saba T, Yiu HHP et al (2017) Cofactor NAD(P)H regeneration inspired by heterogeneous pathways. Chem 2:621–654. https://doi.org/10.1016/j.chempr.2017.04.009
doi: 10.1016/j.chempr.2017.04.009
Demir AS, Talpur FN, Betul Sopaci S et al (2011) Selective oxidation and reduction reactions with cofactor regeneration mediated by galactitol-, lactate-, and formate dehydrogenases immobilized on magnetic nanoparticles. J Biotechnol 152:176–183. https://doi.org/10.1016/j.jbiotec.2011.03.002
doi: 10.1016/j.jbiotec.2011.03.002 pubmed: 21392547
Sheldon RA (2007) Enzyme immobilization: the quest for optimum performance. Adv Synth Catal 349:1289–1307. https://doi.org/10.1002/adsc.200700082
doi: 10.1002/adsc.200700082
Cui JD, Jia SR (2015) Optimization protocols and improved strategies of cross-linked enzyme aggregates technology: current development and future challenges. Crit Rev Biotechnol 35:15–28. https://doi.org/10.3109/07388551.2013.795516
doi: 10.3109/07388551.2013.795516 pubmed: 23886350
Cui JD, Cui LL, Zhang SP et al (2014) Hybrid magnetic cross-linked enzyme aggregates of phenylalanine ammonia lyase from rhodotorula glutinis. PLoS ONE 9:e97221. https://doi.org/10.1371/journal.pone.0097221
doi: 10.1371/journal.pone.0097221 pubmed: 24825453 pmcid: 4019550
Cao L (2005) Immobilised enzymes: science or art? Curr Opin Chem Biol 9:217–226. https://doi.org/10.1016/j.cbpa.2005.02.014
doi: 10.1016/j.cbpa.2005.02.014 pubmed: 15811808
Cao L, van Langen L, Sheldon RA (2003) Immobilised enzymes: carrier-bound or carrier-free? Curr Opin Biotechnol 14:387–394. https://doi.org/10.1016/s0958-1669(03)00096-x
doi: 10.1016/s0958-1669(03)00096-x pubmed: 12943847
Talekar S, Pandharbale A, Ladole M et al (2013) Carrier free co-immobilization of alpha amylase, glucoamylase and pullulanase as combined cross-linked enzyme aggregates (combi-CLEAs): a tri-enzyme biocatalyst with one pot starch hydrolytic activity. Bioresour Technol 147:269–275. https://doi.org/10.1016/j.biortech.2013.08.035
doi: 10.1016/j.biortech.2013.08.035 pubmed: 23999260
Ramos MD, Miranda LP, Giordano RLC et al (2018) 1,3-Regiospecific ethanolysis of soybean oil catalyzed by crosslinked porcine pancreas lipase aggregates. Biotechnol Prog 34:910–920. https://doi.org/10.1002/btpr.2636
doi: 10.1002/btpr.2636 pubmed: 29693317
Cui J, Cui L, Jia S et al (2016) Hybrid cross-linked lipase aggregates with magnetic nanoparticles: a robust and recyclable biocatalysis for the epoxidation of oleic acid. J Agric Food Chem 64:7179–7187. https://doi.org/10.1021/acs.jafc.6b01939
doi: 10.1021/acs.jafc.6b01939 pubmed: 27595982
Cui J, Zhang S, Sun LM (2012) Cross-linked enzyme aggregates of phenylalanine ammonia lyase: novel biocatalysts for synthesis of L-phenylalanine. Appl Biochem Biotechnol 167:835–844. https://doi.org/10.1007/s12010-012-9738-0
doi: 10.1007/s12010-012-9738-0 pubmed: 22622644
Cui J, Zhao Y, Feng Y et al (2017) Encapsulation of spherical cross-linked phenylalanine ammonia lyase aggregates in mesoporous biosilica. J Agric Food Chem 65:618–625. https://doi.org/10.1021/acs.jafc.6b05003
doi: 10.1021/acs.jafc.6b05003 pubmed: 28054483
Cui J, Zhao Y, Tan Z et al (2017) Mesoporous phenylalanine ammonia lyase microspheres with improved stability through calcium carbonate templating. Int J Biol Macromol 98:887–896. https://doi.org/10.1016/j.ijbiomac.2017.02.059
doi: 10.1016/j.ijbiomac.2017.02.059 pubmed: 28219688
Xu M-Q, Li F-L, Yu W-Q et al (2020) Combined cross-linked enzyme aggregates of glycerol dehydrogenase and NADH oxidase for high efficiency in situ NAD
doi: 10.1016/j.ijbiomac.2019.09.178 pubmed: 31669469
Freimund S, Huwig A, Giffhorn F et al (1996) Convenient chemo-enzymatic synthesis of D-tagatose. J Carbohydr Chem 15:115–120. https://doi.org/10.1080/07328309608005430
doi: 10.1080/07328309608005430
Su W-B, Li F-L, Li X-Y et al (2021) Using galactitol dehydrogenase coupled with water-forming NADH oxidase for efficient enzymatic synthesis of L-tagatose. New Biotechnol 62:18–25. https://doi.org/10.1016/j.nbt.2021.01.003
doi: 10.1016/j.nbt.2021.01.003
Li F-L, Shi Y, Zhang J-X et al (2018) Cloning, expression, characterization and homology modeling of a novel water-forming NADH oxidase from Streptococcus mutans ATCC 25175. Int J Biol Macromol 113:1073–1079. https://doi.org/10.1016/j.ijbiomac.2018.03.016
doi: 10.1016/j.ijbiomac.2018.03.016 pubmed: 29514042
Zhuang M-Y, Jiang X-P, Ling X-M et al (2018) Immobilization of glycerol dehydrogenase and NADH oxidase for enzymatic synthesis of 1,3-dihydroxyacetone with in situ cofactor regeneration. J Chem Technol Biotechnol 93:2351–2358. https://doi.org/10.1002/jctb.5579
doi: 10.1002/jctb.5579
Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254. https://doi.org/10.1016/0003-2697(76)90527-3
doi: 10.1016/0003-2697(76)90527-3 pubmed: 942051
Lee D-W, Jang H-J, Choe E-A et al (2004) Characterization of a thermostable L-arabinose (D-galactose) isomerase from the hyperthermophilic eubacterium Thermotoga maritima. Appl Environ Microbiol 70:1397–1404. https://doi.org/10.1128/aem.70.3.1397-1404.2004
doi: 10.1128/aem.70.3.1397-1404.2004 pubmed: 15006759 pmcid: 368370
Mezzenga R, Jung J-M, Adamcik J (2010) Effects of charge double layer and colloidal aggregation on the isotropic-nematic transition of protein fibers in water. Langmuir 26:10401–10405. https://doi.org/10.1021/la101636r
doi: 10.1021/la101636r pubmed: 20509704
Pchelintsev NA, Youshko MI, Švedas VK (2009) Quantitative characteristic of the catalytic properties and microstructure of cross-linked enzyme aggregates of penicillin acylase. J Mol Catal B Enzym 56:202–207. https://doi.org/10.1016/j.molcatb.2008.05.006
doi: 10.1016/j.molcatb.2008.05.006
Aytar B, Bakir U (2008) Preparation of cross-linked tyrosinase aggregates. Process Biochem 43:125–131. https://doi.org/10.1016/j.procbio.2007.11.001
doi: 10.1016/j.procbio.2007.11.001
Nadar S, Muley A, Ladole M et al (2015) Macromolecular cross-linked enzyme aggregates (M-CLEAs) of α-amylase. Int J Biol Macromol 84:69–78. https://doi.org/10.1016/j.ijbiomac.2015.11.082
doi: 10.1016/j.ijbiomac.2015.11.082 pubmed: 26675136
Xu M-Q, Wang S-S, Li L-N et al (2018) Combined cross-linked enzyme aggregates as biocatalysts. Catalysts 8:460. https://doi.org/10.3390/catal8100460
doi: 10.3390/catal8100460
Talekar S, Joshi A, Joshi G et al (2013) Parameters in preparation and characterization of cross linked enzyme aggregates (CLEAs). RSC Adv 3:12485–12511. https://doi.org/10.1039/C3RA40818C
doi: 10.1039/C3RA40818C
Sheldon RA (2011) Cross-linked enzyme aggregates as industrial biocatalysts. Org Process Res Dev 15:213–223. https://doi.org/10.1021/op100289f
doi: 10.1021/op100289f
Mateo C, Palomo JM, van Langen LM et al (2004) A new, mild cross-linking methodology to prepare cross-linked enzyme aggregates. Biotechnol Bioeng 86:273–276. https://doi.org/10.1002/bit.20033
doi: 10.1002/bit.20033 pubmed: 15083507
Arana-Peña S, Carballares D, Morellon-Sterlling R et al (2020) Enzyme co-immobilization: always the biocatalyst designers’ choice…or not? Biotechnol Adv 51:107584. https://doi.org/10.1016/j.biotechadv.2020.107584
doi: 10.1016/j.biotechadv.2020.107584 pubmed: 32668324
Benítez-Mateos A, Nidetzky B, Bolivar J et al (2017) Single-particle studies to advance the characterization of heterogeneous biocatalysts. ChemCatChem 10:654–665. https://doi.org/10.1002/cctc.201701590
doi: 10.1002/cctc.201701590
Wang M, Jia C, Qi W et al (2011) Porous-CLEAs of papain: application to enzymatic hydrolysis of macromolecules. Bioresour Technol 102:3541–3545. https://doi.org/10.1016/j.biortech.2010.08.120
doi: 10.1016/j.biortech.2010.08.120 pubmed: 20863695
Xu D-Y, Chen J-Y, Yang Z (2012) Use of cross-linked tyrosinase aggregates as catalyst for synthesis of L-DOPA. Biochem Eng J 63:88–94. https://doi.org/10.1016/j.bej.2011.11.009
doi: 10.1016/j.bej.2011.11.009
Hanamoto JH, Dupuis P, El-Sayed MA (1984) On the protein (tyrosine)-chromophore (protonated Schiff base) coupling in bacteriorhodopsin. Proc Natl Acad Sci USA 81:7083–7087. https://doi.org/10.1073/pnas.81.22.7083
doi: 10.1073/pnas.81.22.7083 pubmed: 6594682 pmcid: 392081
Wondrak EM, Louis JM, Oroszlan S (1991) The effect of salt on the Michaelis Menten constant of the HIV-1 protease correlates with the Hofmeister series. FEBS Lett 280:344–346. https://doi.org/10.1016/0014-5793(91)80327-Y
doi: 10.1016/0014-5793(91)80327-Y pubmed: 2013335
Zhen Q, Wang M, Qi W et al (2013) Preparation of β-mannanase CLEAs using macromolecular cross-linkers. Catal Sci Technol 3:1937–1941. https://doi.org/10.1039/C3CY20886A
doi: 10.1039/C3CY20886A
Liu Y, Feng Y, Wang L et al (2019) Structural insights into phosphite dehydrogenase variants favoring a non-natural redox cofactor. ACS Catal 9:1883–1887. https://doi.org/10.1021/acscatal.8b04822
doi: 10.1021/acscatal.8b04822
Goetze D, Foletto EF, da Silva HB et al (2017) Effect of feather meal as proteic feeder on combi-CLEAs preparation for grape juice clarification. Process Biochem 62:122–127. https://doi.org/10.1016/j.procbio.2017.07.015
doi: 10.1016/j.procbio.2017.07.015
Iyer PV, Ananthanarayan L (2008) Enzyme stability and stabilization—aqueous and non-aqueous environment. Process Biochem 43:1019–1032. https://doi.org/10.1016/j.procbio.2008.06.004
doi: 10.1016/j.procbio.2008.06.004
Rollini M, Manzoni M (2005) Bioconversion of D-galactitol to tagatose and dehydrogenase activity induction in Gluconobacter oxydans. Process Biochem 40:437–444. https://doi.org/10.1016/j.procbio.2004.01.028
doi: 10.1016/j.procbio.2004.01.028
Jørgensen F, Hansen O, Stougaard P (2004) Enzymatic conversion of D-galactose to D-tagatose: heterologous expression and characterisation of a thermostable L-arabinose isomerase from Thermoanaerobacter mathranii. Appl Microbiol Biotechnol 64:816–822. https://doi.org/10.1007/s00253-004-1578-6
doi: 10.1007/s00253-004-1578-6 pubmed: 15168095

Auteurs

Xue-Yong Li (XY)

School of Pharmacy, Jiangsu University, Zhenjiang, 212013, People's Republic of China.

Meng-Qiu Xu (MQ)

School of Pharmacy, Jiangsu University, Zhenjiang, 212013, People's Republic of China.

Hui Liu (H)

School of Pharmacy, Jiangsu University, Zhenjiang, 212013, People's Republic of China.

Qiang Zhou (Q)

School of Pharmacy, Jiangsu University, Zhenjiang, 212013, People's Republic of China.

Jian Gao (J)

College of Petroleum and Chemical Engineering, Qinzhou, 535100, People's Republic of China.

Ye-Wang Zhang (YW)

School of Pharmacy, Jiangsu University, Zhenjiang, 212013, People's Republic of China. zhangyewang@ujs.edu.cn.

Articles similaires

Regeneration of a Discoid Meniscus: A Case Report.

Myung-Jin Cha, John P Avendano, Aoife MacMahon et al.
1.00
Humans Female Child, Preschool Menisci, Tibial Arthroscopy
Periodontal Ligament Humans Regeneration Stem Cells Animals
Humans Keratoconus Male Cross-Linking Reagents Female
Humans Female Male Middle Aged Aged

Classifications MeSH