Recombinant expression and characterization of the endochitinase Chit36-TA from Trichoderma asperellum in Komagataella phaffii for chitin degradation of black soldier fly exuviae.
Komagataella phaffii
Trichoderma asperellum
Biopolymer
Black soldier fly larvae
Chitin
Chitinases
Journal
Bioprocess and biosystems engineering
ISSN: 1615-7605
Titre abrégé: Bioprocess Biosyst Eng
Pays: Germany
ID NLM: 101088505
Informations de publication
Date de publication:
08 Aug 2024
08 Aug 2024
Historique:
received:
12
02
2024
accepted:
17
07
2024
medline:
8
8
2024
pubmed:
8
8
2024
entrez:
8
8
2024
Statut:
aheadofprint
Résumé
The natural polymer chitin is an abundant source for valuable N-acetylchitooligosaccharides and N-acetylglucosamine applicable in several industries. The endochitinase Chit36-TA from Trichoderma asperellum was recombinantly expressed in Komagataella phaffii for the enzymatic degradation of chitin from unused insect exuviae into N-acetylchitooligosaccharides. Chit36-TA was purified by Ni-NTA affinity chromatography and subsequently biochemically characterized. After deglycosylation, the endochitinase had a molecular weight of 36 kDa. The optimum pH for Chit36-TA was 4.5. The temperature maximum of Chit36-TA was determined to be 50 °C, while it maintained > 93% activity up to 60 °C. The chitinase was thermostable up to 45 °C and exhibited ~ 50% activity after a 15 min incubation at 57 °C. Chit36-TA had a maximum specific enzyme activity of 50 nkat/mg with a K
Identifiants
pubmed: 39115691
doi: 10.1007/s00449-024-03067-4
pii: 10.1007/s00449-024-03067-4
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Deutsche Forschungsgemeinschaft
ID : 466169172
Organisme : Deutsche Forschungsgemeinschaft
ID : 466169172
Organisme : Deutsche Forschungsgemeinschaft
ID : 466169172
Organisme : Deutsche Forschungsgemeinschaft
ID : 466169172
Organisme : Deutsche Forschungsgemeinschaft
ID : 466169172
Organisme : National Science Centre, Poland
ID : UMO-2020/39/I/NZ9/00907
Informations de copyright
© 2024. The Author(s).
Références
Hahn T, Tafi E, Paul A et al (2020) Current state of chitin purification and chitosan production from insects. J Chem Technol Biotechnol 95:2775–2795. https://doi.org/10.1002/jctb.6533
doi: 10.1002/jctb.6533
Dwyer K, Bentley IS, Fitzpatrick DA et al (2023) Recombinant production, characterization and industrial application testing of a novel acidic exo/endo-chitinase from Rasamsonia emersonii. Extremophiles 27:10. https://doi.org/10.1007/s00792-023-01293-4
doi: 10.1007/s00792-023-01293-4
pubmed: 37071215
Ngo D-N, Lee S-H, Kim M-M et al (2009) Production of chitin oligosaccharides with different molecular weights and their antioxidant effect in RAW 264.7 cells. Journal of Functional Foods 1:188–198. https://doi.org/10.1016/j.jff.2009.01.008
doi: 10.1016/j.jff.2009.01.008
Katano H, Noba S, Sato K et al (2017) Solubility-based separation and purification of long-chain chitin oligosaccharides with organic-water mixed solvent. Analy Sci. https://doi.org/10.2116/analsci.33.639
doi: 10.2116/analsci.33.639
van Broek LAM den, Boeriu CG, Stevens CV (eds) (2020) Chitin and chitosan: Properties and applications. Wiley series in renewable resource. Wiley, Hoboken NJ
Shamshina JL, Kelly A, Oldham T et al (2020) Agricultural uses of chitin polymers. Environ Chem Lett 18:53–60. https://doi.org/10.1007/s10311-019-00934-5
doi: 10.1007/s10311-019-00934-5
Barikani M, Oliaei E, Seddiqi H et al (2014) Preparation and application of chitin and its derivatives: a review. Iran Polym J 23:307–326. https://doi.org/10.1007/s13726-014-0225-z
doi: 10.1007/s13726-014-0225-z
Zhang R, Zhao Q, Yi Z et al (2023) Chitin oligosaccharides for the food industry: production and applications. Syst Microbiol and Biomanuf 3:49–74. https://doi.org/10.1007/s43393-022-00127-2
doi: 10.1007/s43393-022-00127-2
Kerton FM, Yan N (eds) (2017) Fuels, Chemicals and Materials from the Oceans and Aquatic Sources, 1
United Nations, Department of Economic and Social Affairs, Population Division (2019) World Population Prospects 2019 Highlights https://doi.org/10.18356/13bf5476-en
Marono S, Piccolo G, Loponte R et al (2016) In vitro crude protein digestibility of Tenebrio molitor and Hermetia illucens insect meals and its correlation with chemical composition traits. Ital J Anim Sci 14:3889. https://doi.org/10.4081/ijas.2015.3889
doi: 10.4081/ijas.2015.3889
Caparros Megido R, Francis F, Haubruge E et al (2024) A worldwide overview of the status and prospects of edible insect production. Entomologia. https://doi.org/10.1127/entomologia/2023/2279
doi: 10.1127/entomologia/2023/2279
Conway A, Jaiswal S, Jaiswal AK (2024) The potential of edible insects as a safe, palatable, and sustainable food source in the European Union. Foods. https://doi.org/10.3390/foods13030387
Hahn T, Tafi E, von Seggern N et al (2022) Purification of chitin from pupal exuviae of the black soldier fly. Waste Biomass Valor 13:1993–2008. https://doi.org/10.1007/s12649-021-01645-1
doi: 10.1007/s12649-021-01645-1
Spranghers T, Ottoboni M, Klootwijk C et al (2017) Nutritional composition of black soldier fly (Hermetia illucens) prepupae reared on different organic waste substrates. J Sci Food Agric 97:2594–2600. https://doi.org/10.1002/jsfa.8081
doi: 10.1002/jsfa.8081
pubmed: 27734508
Finke MD (2015) Complete nutrient content of four species of commercially available feeder insects fed enhanced diets during growth. Zoo Biol 34:554–564. https://doi.org/10.1002/zoo.21246
doi: 10.1002/zoo.21246
pubmed: 26366856
Rehman, K.u., Hollah, C., Wiesotzki, K. et al (2023) Insect-derived chitin and chitosan: a still unexploited resource for the edible insect sector. Sustainability 15:4864–4898. https://doi.org/10.3390/su15064864
doi: 10.3390/su15064864
Patra JK, Das G, Shin H-S (eds) (2018) Microbial Biotechnology: Volume 2. Application in Food and Pharmacology. Springer eBook Collection. Springer Singapore, Singapore
Abidin MZ, Junqueira-Gonçalves MP, Khutoryanskiy VV et al (2017) Intensifying chitin hydrolysis by adjunct treatments - an overview. J Chem Technol Biotechnol 92:2787–2798. https://doi.org/10.1002/jctb.5208
doi: 10.1002/jctb.5208
Adrangi S, Faramarzi MA (2013) From bacteria to human: a journey into the world of chitinases. Biotechnol Adv 31:1786–1795. https://doi.org/10.1016/j.biotechadv.2013.09.012
doi: 10.1016/j.biotechadv.2013.09.012
pubmed: 24095741
Rea S (2020) Chitin chitinases and chitin derivatives in biopharmaceutical agricultural and environmental perspective. Biointerface Res Appl Chem. https://doi.org/10.33263/BRIAC113.998510005
doi: 10.33263/BRIAC113.998510005
Erden-Karaoğlan F, Karaoğlan M (2022) Applicability of the heterologous yeast promoters for recombinant protein production in Pichia pastoris. Appl Microbiol Biotechnol 106:7073–7083. https://doi.org/10.1007/s00253-022-12183-8
doi: 10.1007/s00253-022-12183-8
pubmed: 36163554
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. https://doi.org/10.1016/0003-2697(76)90527-3
doi: 10.1016/0003-2697(76)90527-3
pubmed: 942051
Laemmli UK (1979) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. https://doi.org/10.1038/227680a0
doi: 10.1038/227680a0
Songsiriritthigul C, Lapboonrueng S, Pechsrichuang P et al (2010) Expression and characterization of Bacillus licheniformis chitinase (ChiA), suitable for bioconversion of chitin waste. Bioresour Technol 101:4096–4103. https://doi.org/10.1016/j.biortech.2010.01.036
doi: 10.1016/j.biortech.2010.01.036
pubmed: 20133129
Pérez-Martínez AS, de León-Rodríguez A, Harris LJ et al (2007) Overexpression, purification and characterization of the Trichoderma atroviride endochitinase, Ech42, in Pichia pastoris. Protein Expr Purif 55:183–188. https://doi.org/10.1016/j.pep.2007.05.009
doi: 10.1016/j.pep.2007.05.009
pubmed: 17629497
McCreath KJ, Gooday GW (1992) A rapid and sensitive microassay for determination of chitinolytic activity. J Microbiol Methods 14(4):229–237
doi: 10.1016/0167-7012(92)90055-9
Bisswanger H (2008) Enzyme kinetics: Principles and methods, 2nd. rev. and updated ed. Wiley-VCH, Weinheim (Federal Republic of Germany)
Schneider L, Schuh- von Graevenitz H, Wiltafsky-Martin M et al. (2024) Effect of protein content in isoenergetic diets on energy, nitrogen, and amino acid retention of the Black Soldier Fly Larvae (BSFL; Hermetia illucens L.): [Presentation]. Society of Nutrition Physiology : 78th Conference 05th– 07th March 2024 in Göttingen, Proceedings of the Society of Nutrition Physiology.
Akeed Y, Atrash F, Naffaa W (2020) Partial purification and characterization of chitinase produced by Bacillus licheniformis B307. Heliyon 6:e03858. https://doi.org/10.1016/j.heliyon.2020.e03858
doi: 10.1016/j.heliyon.2020.e03858
pubmed: 32395650
pmcid: 7205749
Ali R, El-Boubbou K, Boudjelal M (2021) An easy, fast and inexpensive method of preparing a biological specimen for scanning electron microscopy (SEM). MethodsX 8:101521. https://doi.org/10.1016/j.mex.2021.101521
doi: 10.1016/j.mex.2021.101521
pubmed: 34754792
pmcid: 8564727
Fan Y, Zhang Y, Yang X et al (2007) Expression of a Beauveria bassiana chitinase (Bbchit1) in Escherichia coli and Pichia pastoris. Protein Expr Purif 56:93–99. https://doi.org/10.1016/j.pep.2007.06.012
doi: 10.1016/j.pep.2007.06.012
pubmed: 17692532
Fitches E, Wilkinson H, Bell H et al (2004) Cloning, expression and functional characterisation of chitinase from larvae of tomato moth (Lacanobia oleracea): a demonstration of the insecticidal activity of insect chitinase. Insect Biochem Mol Biol 34:1037–1050. https://doi.org/10.1016/j.ibmb.2004.06.012
doi: 10.1016/j.ibmb.2004.06.012
pubmed: 15475298
Kidibule PE, Santos-Moriano P, Plou FJ et al (2020) Endo-chitinase Chit33 specificity on different chitinolytic materials allows the production of unexplored chitooligosaccharides with antioxidant activity. Biotechnol Rep (Amst) 27:e00500. https://doi.org/10.1016/j.btre.2020.e00500
doi: 10.1016/j.btre.2020.e00500
pubmed: 32685384
Yu P, Tang Y (2012) Construction of the highly secreted endochitinase Pichia pastoris strain and the optimization of chitin-degrading conditions. Carbohydr Polym 89:41–45. https://doi.org/10.1016/j.carbpol.2012.02.034
doi: 10.1016/j.carbpol.2012.02.034
pubmed: 24750601
Lee SG, Koh HY, Han SJ et al (2010) Expression of recombinant endochitinase from the Antarctic bacterium, Sanguibacter antarcticus KOPRI 21702 in Pichia pastoris by codon optimization. Protein Expr Purif 71:108–114. https://doi.org/10.1016/j.pep.2010.01.017
doi: 10.1016/j.pep.2010.01.017
pubmed: 20100576
Kidibule PE, Santos-Moriano P, Jiménez-Ortega E et al (2018) Use of chitin and chitosan to produce new chitooligosaccharides by chitinase Chit42: enzymatic activity and structural basis of protein specificity. Microb Cell Fact 17:47. https://doi.org/10.1186/s12934-018-0895-x
doi: 10.1186/s12934-018-0895-x
pubmed: 29566690
pmcid: 5863366
Song W, Zhang N, Yang M et al (2020) Multiple strategies to improve the yield of chitinase a from Bacillus licheniformis in Pichia pastoris to obtain plant growth enhancer and GlcNAc. Microb Cell Fact 19:181. https://doi.org/10.1186/s12934-020-01440-y
doi: 10.1186/s12934-020-01440-y
pubmed: 32933546
pmcid: 7493387
Pérez-Martínez AS, La Barba de Rosa AP, León-Rodríguez A (2014) Heterologous expression of Trichoderma atroviride endochitinase ech42 in Pichia pastoris at low and high dissolved oxygen tensions. Revista Mexicana de Ingeniería Química:93–101
Hoell IA, Klemsdal SS, Vaaje-Kolstad G et al (2005) Overexpression and characterization of a novel chitinase from Trichoderma atroviride strain P1. Biochem Biophys Acta 1748:180–190. https://doi.org/10.1016/j.bbapap.2005.01.002
doi: 10.1016/j.bbapap.2005.01.002
pubmed: 15769595
Viterbo A, Montero M, Ramot O et al (2002) Expression regulation of the endochitinase chit36 from Trichoderma asperellum (T. harzianum T-203). Curr Genet 42:114–122. https://doi.org/10.1007/s00294-002-0345-4
doi: 10.1007/s00294-002-0345-4
pubmed: 12478390
Morales-Ruiz E, Priego-Rivera R, Figueroa-López AM et al (2021) Biochemical characterization of two chitinases from Bacillus cereus sensu lato B25 with antifungal activity against Fusarium verticillioides P03. FEMS Microbiol Lett. https://doi.org/10.1093/femsle/fnaa218
doi: 10.1093/femsle/fnaa218
pubmed: 33351136
Yan Q, Fong SS (2018) Cloning and characterization of a chitinase from Thermobifida fusca reveals Tfu_0580 as a thermostable and acidic endochitinase. Biotechnol Rep (Amst) 19:e00274. https://doi.org/10.1016/j.btre.2018.e00274
doi: 10.1016/j.btre.2018.e00274
pubmed: 30094208
Li RK, Hu YJ, He YJ et al (2021) A thermophilic chitinase 1602 from the marine bacterium Microbulbifer sp. BN3 and its high-level expression in Pichia pastoris. Biotechnol Appl Biochem 68:1076–1085. https://doi.org/10.1002/bab.2027
doi: 10.1002/bab.2027
pubmed: 32924196
Mordasini T, Curioni A, Andreoni W (2003) Why do divalent metal ions either promote or inhibit enzymatic reactions? The case of BamHI restriction endonuclease from combined quantum-classical simulations. J Biol Chem 278:4381–4384. https://doi.org/10.1074/jbc.C200664200
doi: 10.1074/jbc.C200664200
pubmed: 12496295
Ahmed U, Pfannstiel J, Stressler T et al (2022) Purification and characterization of a fungal aspartic peptidase from Trichoderma reesei and its application for food and animal feed protein hydrolyses. J Sci Food Agric 102:5190–5199. https://doi.org/10.1002/jsfa.11871
doi: 10.1002/jsfa.11871
pubmed: 35289936
Nguyen HA, Nguyen T-H, Nguyen T-T et al (2012) Chitinase from Bacillus licheniformis DSM13: expression in Lactobacillus plantarum WCFS1 and biochemical characterisation. Protein Expr Purif 81:166–174. https://doi.org/10.1016/j.pep.2011.10.005
doi: 10.1016/j.pep.2011.10.005
pubmed: 22037312
Moussian B (2010) Recent advances in understanding mechanisms of insect cuticle differentiation. Insect Biochem Mol Biol 40:363–375. https://doi.org/10.1016/j.ibmb.2010.03.003
doi: 10.1016/j.ibmb.2010.03.003
pubmed: 20347980
Teixeira RSS, Da Silva AS, Ferreira-Leitão VS et al (2012) Amino acids interference on the quantification of reducing sugars by the 3,5-dinitrosalicylic acid assay mislead carbohydrase activity measurements. Carbohydr Res 363:33–37. https://doi.org/10.1016/j.carres.2012.09.024
doi: 10.1016/j.carres.2012.09.024
pubmed: 23103512