Identification of a novel tailor-made chitinase from white shrimp fenneropenaeus merguiensis

Fenneropenaeus merguiensis (commonly named banana shrimp) is one of the most important farmed crustacean worldwide species for the fisheries and aquaculture industry. Besides its nutritional value, it is a good source of chitinase, an enzyme with excellent biological and catalytic properties for man...

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Autores:: Beygmoradi, Azadeh
Homaei, Ahmad
Hemmati, Roohullah
Del Arco, Jon
Fernández-Lucas, Jesús

Tipo de recurso:: http://purl.org/coar/resource_type/c_816b

Fecha de publicación:: 2021

Institución:: Corporación Universidad de la Costa

Repositorio:: REDICUC - Repositorio CUC

Idioma:: eng

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network_acronym_str	RCUC2
network_name_str	REDICUC - Repositorio CUC
repository_id_str
dc.title.spa.fl_str_mv	Identification of a novel tailor-made chitinase from white shrimp fenneropenaeus merguiensis
title	Identification of a novel tailor-made chitinase from white shrimp fenneropenaeus merguiensis
spellingShingle	Identification of a novel tailor-made chitinase from white shrimp fenneropenaeus merguiensis Marine organisms Chitinolitic enzymes Molecular cloning Protein purification Biochemical characterization
title_short	Identification of a novel tailor-made chitinase from white shrimp fenneropenaeus merguiensis
title_full	Identification of a novel tailor-made chitinase from white shrimp fenneropenaeus merguiensis
title_fullStr	Identification of a novel tailor-made chitinase from white shrimp fenneropenaeus merguiensis
title_full_unstemmed	Identification of a novel tailor-made chitinase from white shrimp fenneropenaeus merguiensis
title_sort	Identification of a novel tailor-made chitinase from white shrimp fenneropenaeus merguiensis
dc.creator.fl_str_mv	Beygmoradi, Azadeh Homaei, Ahmad Hemmati, Roohullah Del Arco, Jon Fernández-Lucas, Jesús
dc.contributor.author.spa.fl_str_mv	Beygmoradi, Azadeh Homaei, Ahmad Hemmati, Roohullah Del Arco, Jon Fernández-Lucas, Jesús
dc.subject.spa.fl_str_mv	Marine organisms Chitinolitic enzymes Molecular cloning Protein purification Biochemical characterization
topic	Marine organisms Chitinolitic enzymes Molecular cloning Protein purification Biochemical characterization
description	Fenneropenaeus merguiensis (commonly named banana shrimp) is one of the most important farmed crustacean worldwide species for the fisheries and aquaculture industry. Besides its nutritional value, it is a good source of chitinase, an enzyme with excellent biological and catalytic properties for many industrial applications. In the present study, a putative chitinase-encoding cDNA was synthesized from mRNA from F. merguiensis hepatopancreas tissue. Subsequently, the corresponding cDNA was cloned, sequenced and functionally expressed in Escherichia coli, and the recombinant F. merguiensis chitinase (rFmCHI) was purified by His-tag affinity chromatography. The bioinformatics analysis of aminoacid sequence of rFmCHI displayed a cannonical multidomain architecture in chitinases which belongs to glycoside hydrolase family 18 (GH18 chitinase). Biochemical characterization revealed rFmCHI as a monomeric enzyme of molecular weight 52 kDa with maximum activity at 40 °C and pH 6.0 Moreover, the recombinant enzyme is also stable up to 60 °C, and in the pH range 5.0-8.0. Steady-state kinetic studies for colloidal chitin revealed KM, Vmax and kcat values of 78.18 μM, 0.07261 μM. min−1 and 43.37 s−1, respectively. Overall, our results aim to demonstrate the potential of rFmCHI as suitable catalyst for bioconversion of chitin waste.
publishDate	2021
dc.date.accessioned.none.fl_str_mv	2021-05-04T23:30:55Z
dc.date.available.none.fl_str_mv	2021-05-04T23:30:55Z
dc.date.issued.none.fl_str_mv	2021
dc.date.embargoEnd.none.fl_str_mv	2023
dc.type.spa.fl_str_mv	Pre-Publicación
dc.type.coar.spa.fl_str_mv	http://purl.org/coar/resource_type/c_816b
dc.type.content.spa.fl_str_mv	Text
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dc.identifier.issn.spa.fl_str_mv	0927-7765 1873-4367
dc.identifier.uri.spa.fl_str_mv	https://hdl.handle.net/11323/8221
dc.identifier.doi.spa.fl_str_mv	https://doi.org/10.1016/j.colsurfb.2021.111747
dc.identifier.instname.spa.fl_str_mv	Corporación Universidad de la Costa
dc.identifier.reponame.spa.fl_str_mv	REDICUC - Repositorio CUC
dc.identifier.repourl.spa.fl_str_mv	https://repositorio.cuc.edu.co/
identifier_str_mv	0927-7765 1873-4367 Corporación Universidad de la Costa REDICUC - Repositorio CUC
url	https://hdl.handle.net/11323/8221 https://doi.org/10.1016/j.colsurfb.2021.111747 https://repositorio.cuc.edu.co/
dc.language.iso.none.fl_str_mv	eng
language	eng
dc.relation.references.spa.fl_str_mv	[1] S.M. Moss, D.R. Moss, S.M. Arce, D.V. Lightner, J.M. Lotz, The role of selective breeding and biosecurity in the prevention of disease in penaeid shrimp aquaculture, J. Invertebr. Pathol. 110 (2012) 247–250. [2] A. Homaei, Purification and biochemical properties of highly efficient alkaline phosphatase from Fenneropenaeus merguiensis brain, J. Mol. Catal. B Enzym. 118 (2015) 16–22. [3] D.J. Vance, P.C. Rothlisberg, The biology and ecology of the banana prawns: Penaeus merguiensis de Man and P. indicus H. Milne Edwards, Adv. Mar. Biol. 86 (2020) 1–139. [4] A. Beygmoradi, A. Homaei, R. Hemmati, P. Santos-Moriano, D. Hormigo, J. Fernandez-Lucas, Marine chitinolytic enzymes, a biotechnological treasure´ hidden in the ocean? Appl. Microbiol. Biotechnol. 102 (2018) 9937–9948. [5] H.P. Ramesh, R.N. Tharanathan, Carbohydrates—the renewable raw materials of high biotechnological value, Crit. Rev. Biotechnol. 23 (2003) 149–173. [6] Q.-S. Huang, X.-L. Xie, G. Liang, F. Gong, Y. Wang, X.-Q. Wei, Q. Wang, Z.-L. Ji, Q.- X. Chen, The GH18 family of chitinases: their domain architectures, functions and evolutions, Glycobiology 22 (2012) 23–34. [7] J. Zhang, Y. Sun, F. Li, B. Huang, J. Xiang, Molecular characterization and expression analysis of chitinase (Fcchi-3) from Chinese shrimp, Fenneropenaeus chinensis, Mol. Biol. Rep. 37 (2010) 1913–1921. [8] Y. Huang, F. Ma, W. Wang, Q. Ren, Identification and molecular characterization of a peritrophin-like gene, involved in the antibacterial response in Chinese mitten crab, Eriocheir sinensis, Dev. Comp. Immunol. 50 (2015) 129–138. [9] P.K. Dutta, J. Dutta, V. Tripathi, Chitin and Chitosan: Chemistry, Properties and Applications, 2004. [10] I. Hamed, F. Ozogul, J.M. Regenstein, Industrial applications of crustacean by-¨ products (chitin, chitosan, and chitooligosaccharides): a review, Trends Food Sci. Technol. 48 (2016) 40–50. [11] A. Beygmoradi, A. Homaei, Marine microbes as a valuable resource for brand new industrial biocatalysts, Biocatal. Agric. Biotechnol. 11 (2017) 131–152. [12] P.E. Kidibule, P. Santos-Moriano, E. Jim´enez-Ortega, M. Ramírez-Escudero, M. C. Limon, M. Remacha, F.J. Plou, J. Sanz-Aparicio, M. Fer´ nandez-Lobato, Use of´ chitin and chitosan to produce new chitooligosaccharides by chitinase Chit42: enzymatic activity and structural basis of protein specificity, Microb. Cell Fact. 17 (2018) 47. [13] L. Hartl, S. Zach, V. Seidl-Seiboth, Fungal chitinases: diversity, mechanistic properties and biotechnological potential, Appl. Microbiol. Biotechnol. 93 (2012) 533–543. [14] R.S. Patil, V. Ghormade, M.V. Deshpande, Chitinolytic enzymes: an exploration, Enzyme Microb. Technol. 26 (2000) 473–483. [15] S.S. Paulsen, B. Andersen, L. Gram, H. Machado, Biological potential of chitinolytic marine bacteria, Mar. Drugs 14 (2016) 230. [16] T. Fukamizo, Chitinolytic enzymes catalysis, substrate binding, and their application, Curr. Protein Pept. Sci. 1 (2000) 105–124. [17] T. Ohno, S. Armand, T. Hata, N. Nikaidou, B. Henrissat, M. Mitsutomi, T. Watanabe, A modular family 19 chitinase found in the prokaryotic organism Streptomyces griseus HUT 6037, J. Bacteriol. 178 (1996) 5065–5070. [18] A. Kasprzewska, Plant chitinases-regulation and function, Cell. Mol. Biol. Lett. 8 (2003) 809–824. [19] F. Fusetti, H. von Moeller, D. Houston, H.J. Rozeboom, B.W. Dijkstra, R.G. Boot, J. M. Aerts, D.M. van Aalten, Structure of human chitotriosidase implications for specific inhibitor design and function of mammalian chitinase-like lectins, J. Biol. Chem. 277 (2002) 25537–25544. [20] M.R. Stam, E. Blanc, P.M. Coutinho, B. Henrissat, Evolutionary and mechanistic relationships between glycosidases acting on α-and β-bonds, Carbohydr. Res. 340 (2005) 2728–2734. [21] A. Bendt, H. Hüller, U. Kammel, E. Helmke, T. Schweder, Cloning, experssion, and characterization of a chitinase gene from the Antarctic psychrotolerant bacterium Vibrio sp. strain Fi:7, Extremophiles 5 (2001) 119–126. [22] M.M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72 (1976) 248–254. [23] J.D. Thompson, Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice, Nucleic Acids Res. 22 (1994) 4673–4680. [24] S. Kumar, K. Tamura, M. Nei, MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment, Brief. Bioinformatics 5 (2004) 150–163. [25] M. Biasini, S. Bienert, A. Waterhouse, K. Arnold, G. Studer, T. Schmidt, F. Kiefer, T. G. Cassarino, M. Bertoni, L. Bordoli, SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information, Nucleic Acids Res. 42 (2014) W252–W258. [26] D. Case, T. Darden, T. Cheatham III, C. Simmerling, J. Wang, R. Duke, R. Luo, R. Walker, W. Zhang, K. Merz, AMBER 12, University of California, San Francisco, 2010, pp. 1–826, 2012, There is no corresponding record for this reference.[Google Scholar]. [27] R.L. Tellam, Protein motifs in filarial chitinases: an alter-native view, Parasitol. Today 12 (1996) 291–292. [28] Q. Zhu, Y. Deng, P. Vanka, S.J. Brown, S. Muthukrishnan, K.J. Kramer, Computational identification of novel chitinase-like proteins in the Drosophila melanogaster genome, Bioinformatics 20 (2004) 161–169. [29] Z. Shen, M. Jacobs-Lorena, Evolution of chitin-binding proteins in invertebrates, J. Mol. Evol. 48 (1999) 341–347. [30] Y. Arakane, Q. Zhu, M. Matsumiya, S. Muthukrishnan, K.J. Kramer, Properties of catalytic, linker and chitin-binding domains of insect chitinase, Insect Biochem. Mol. Biol. 33 (2003) 631–648. [31] M. Quentin, M. Ebbelaar, J. Derksen, C. Mariani, H. van Der Valk, Description of a cellulose-binding domain and a linker sequence from Aspergillus fungi, Appl. Microbiol. Biotechnol. 58 (2002) 658–662. [32] M. Rechsteiner, S.W. Rogers, PEST sequences and regulation by proteolysis, Trends Biochem. Sci. 21 (1996) 267–271. [33] R. Sotelo-Mundo, E. Moran-Palacio, K. García-Orozco, C. Figueroa-Soto, M. Romo-´ Figueroa, E. Valenzuela-Soto, G. Yepiz-Plascencia, Kinetic characterization, expression and molecular modeling of a chitinase from the pacific white shrimp Litopenaeus vannamei, J. Food Biochem. 33 (2009) 246–259. [34] M. Kono, T. Matsui, C. Shimizu, D. Koga, Purifications and some properties of chitinase from the liver of a prawn, Penaeus japonicus, Agric. Biol. Chem. 54 (1990) 2145–2147. [35] X.-L. Xie, Q.-X. Chen, J.-C. Lin, Y. Wang, Purification and some properties of β-N- acetyl-D-glucosaminidase from prawn (Penaeus vannamei), Mar. Biol. 146 (2004) 143–148. [36] D. Koga, K. Mizuki, A. Ide, M. Kono, T. Matsui, C. Shimizu, Kinetics of a chitinase from a prawn, Penaeus japonicus, Agric. Biol. Chem. 54 (1990) 2505–2512. [37] F. Shojaei, A. Homaei, M.R. Taherizadeh, E. Kamrani, Characterization of biosynthesized chitosan nanoparticles from Penaeus vannamei for the immobilization of P. vannamei protease: an eco-friendly nanobiocatalyst, Int. J. Food Prop. 20 (2017) 1413–1423. [38] R.S. Rasmussen, M.T. Morrissey, Marine biotechnology for production of food ingredients, Adv. Food Nutr. Res. 52 (2007) 237–292. [39] M. Hayes, B. Carney, J. Slater, W. Brück, Mining marine shellfish wastes for bioactive molecules: chitin and chitosan–part B: applications, Biotechnol. J.: Healthcare Nutr. Technol. 3 (2008) 878–889. [40] K. Kurita, Chitin and chitosan: functional biopolymers from marine crustaceans, Mar. Biotechnol. 8 (2006) 203–226. [41] M. Revathi, R. Saravanan, A. Shanmugam, Production and Characterization of Chitinase from Vibrio species, A Head Waste of Shrimp Metapenaeus dobsonii (Miers, 1878) and Chitin of Sepiella inermis Orbigny, 1848, 2012. [42] D. Koga, Application of chitinase in agriculture, J. Met. Mater. Miner 15 (2005) 33–36.
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spelling	Beygmoradi, AzadehHomaei, AhmadHemmati, RoohullahDel Arco, JonFernández-Lucas, Jesús2021-05-04T23:30:55Z2021-05-04T23:30:55Z202120230927-77651873-4367https://hdl.handle.net/11323/8221https://doi.org/10.1016/j.colsurfb.2021.111747Corporación Universidad de la CostaREDICUC - Repositorio CUChttps://repositorio.cuc.edu.co/Fenneropenaeus merguiensis (commonly named banana shrimp) is one of the most important farmed crustacean worldwide species for the fisheries and aquaculture industry. Besides its nutritional value, it is a good source of chitinase, an enzyme with excellent biological and catalytic properties for many industrial applications. In the present study, a putative chitinase-encoding cDNA was synthesized from mRNA from F. merguiensis hepatopancreas tissue. Subsequently, the corresponding cDNA was cloned, sequenced and functionally expressed in Escherichia coli, and the recombinant F. merguiensis chitinase (rFmCHI) was purified by His-tag affinity chromatography. The bioinformatics analysis of aminoacid sequence of rFmCHI displayed a cannonical multidomain architecture in chitinases which belongs to glycoside hydrolase family 18 (GH18 chitinase). Biochemical characterization revealed rFmCHI as a monomeric enzyme of molecular weight 52 kDa with maximum activity at 40 °C and pH 6.0 Moreover, the recombinant enzyme is also stable up to 60 °C, and in the pH range 5.0-8.0. Steady-state kinetic studies for colloidal chitin revealed KM, Vmax and kcat values of 78.18 μM, 0.07261 μM. min−1 and 43.37 s−1, respectively. Overall, our results aim to demonstrate the potential of rFmCHI as suitable catalyst for bioconversion of chitin waste.Beygmoradi, AzadehHomaei, Ahmad-will be generated-orcid-0000-0001-9909-4761-600Hemmati, RoohullahDel Arco, Jon-will be generated-orcid-0000-0003-4646-492X-600Fernández-Lucas, Jesús-will be generated-orcid-0000-0001-7045-8306-600application/pdfengCorporación Universidad de la CostaCC0 1.0 Universalhttp://creativecommons.org/publicdomain/zero/1.0/info:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2Colloids and Surfaces B: Biointerfaceshttps://www.sciencedirect.com/science/article/pii/S0927776521001910?via%3DihubMarine organismsChitinolitic enzymesMolecular cloningProtein purificationBiochemical characterizationIdentification of a novel tailor-made chitinase from white shrimp fenneropenaeus merguiensisPre-Publicaciónhttp://purl.org/coar/resource_type/c_816bTextinfo:eu-repo/semantics/preprinthttp://purl.org/redcol/resource_type/ARTOTRinfo:eu-repo/semantics/acceptedVersion[1] S.M. Moss, D.R. Moss, S.M. Arce, D.V. Lightner, J.M. Lotz, The role of selective breeding and biosecurity in the prevention of disease in penaeid shrimp aquaculture, J. Invertebr. Pathol. 110 (2012) 247–250.[2] A. Homaei, Purification and biochemical properties of highly efficient alkaline phosphatase from Fenneropenaeus merguiensis brain, J. Mol. Catal. B Enzym. 118 (2015) 16–22.[3] D.J. Vance, P.C. Rothlisberg, The biology and ecology of the banana prawns: Penaeus merguiensis de Man and P. indicus H. Milne Edwards, Adv. Mar. Biol. 86 (2020) 1–139.[4] A. Beygmoradi, A. Homaei, R. Hemmati, P. Santos-Moriano, D. Hormigo, J. Fernandez-Lucas, Marine chitinolytic enzymes, a biotechnological treasure´ hidden in the ocean? Appl. Microbiol. Biotechnol. 102 (2018) 9937–9948.[5] H.P. Ramesh, R.N. Tharanathan, Carbohydrates—the renewable raw materials of high biotechnological value, Crit. Rev. Biotechnol. 23 (2003) 149–173.[6] Q.-S. Huang, X.-L. Xie, G. Liang, F. Gong, Y. Wang, X.-Q. Wei, Q. Wang, Z.-L. Ji, Q.- X. Chen, The GH18 family of chitinases: their domain architectures, functions and evolutions, Glycobiology 22 (2012) 23–34.[7] J. Zhang, Y. Sun, F. Li, B. Huang, J. Xiang, Molecular characterization and expression analysis of chitinase (Fcchi-3) from Chinese shrimp, Fenneropenaeus chinensis, Mol. Biol. Rep. 37 (2010) 1913–1921.[8] Y. Huang, F. Ma, W. Wang, Q. Ren, Identification and molecular characterization of a peritrophin-like gene, involved in the antibacterial response in Chinese mitten crab, Eriocheir sinensis, Dev. Comp. Immunol. 50 (2015) 129–138.[9] P.K. Dutta, J. Dutta, V. Tripathi, Chitin and Chitosan: Chemistry, Properties and Applications, 2004.[10] I. Hamed, F. Ozogul, J.M. Regenstein, Industrial applications of crustacean by-¨ products (chitin, chitosan, and chitooligosaccharides): a review, Trends Food Sci. Technol. 48 (2016) 40–50.[11] A. Beygmoradi, A. Homaei, Marine microbes as a valuable resource for brand new industrial biocatalysts, Biocatal. Agric. Biotechnol. 11 (2017) 131–152.[12] P.E. Kidibule, P. Santos-Moriano, E. Jim´enez-Ortega, M. Ramírez-Escudero, M. C. Limon, M. Remacha, F.J. Plou, J. Sanz-Aparicio, M. Fer´ nandez-Lobato, Use of´ chitin and chitosan to produce new chitooligosaccharides by chitinase Chit42: enzymatic activity and structural basis of protein specificity, Microb. Cell Fact. 17 (2018) 47.[13] L. Hartl, S. Zach, V. Seidl-Seiboth, Fungal chitinases: diversity, mechanistic properties and biotechnological potential, Appl. Microbiol. Biotechnol. 93 (2012) 533–543.[14] R.S. Patil, V. Ghormade, M.V. Deshpande, Chitinolytic enzymes: an exploration, Enzyme Microb. Technol. 26 (2000) 473–483.[15] S.S. Paulsen, B. Andersen, L. Gram, H. Machado, Biological potential of chitinolytic marine bacteria, Mar. Drugs 14 (2016) 230.[16] T. Fukamizo, Chitinolytic enzymes catalysis, substrate binding, and their application, Curr. Protein Pept. Sci. 1 (2000) 105–124.[17] T. Ohno, S. Armand, T. Hata, N. Nikaidou, B. Henrissat, M. Mitsutomi, T. Watanabe, A modular family 19 chitinase found in the prokaryotic organism Streptomyces griseus HUT 6037, J. Bacteriol. 178 (1996) 5065–5070.[18] A. Kasprzewska, Plant chitinases-regulation and function, Cell. Mol. Biol. Lett. 8 (2003) 809–824.[19] F. Fusetti, H. von Moeller, D. Houston, H.J. Rozeboom, B.W. Dijkstra, R.G. Boot, J. M. Aerts, D.M. van Aalten, Structure of human chitotriosidase implications for specific inhibitor design and function of mammalian chitinase-like lectins, J. Biol. Chem. 277 (2002) 25537–25544.[20] M.R. Stam, E. Blanc, P.M. Coutinho, B. Henrissat, Evolutionary and mechanistic relationships between glycosidases acting on α-and β-bonds, Carbohydr. Res. 340 (2005) 2728–2734.[21] A. Bendt, H. Hüller, U. Kammel, E. Helmke, T. Schweder, Cloning, experssion, and characterization of a chitinase gene from the Antarctic psychrotolerant bacterium Vibrio sp. strain Fi:7, Extremophiles 5 (2001) 119–126.[22] M.M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72 (1976) 248–254.[23] J.D. Thompson, Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice, Nucleic Acids Res. 22 (1994) 4673–4680.[24] S. Kumar, K. Tamura, M. Nei, MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment, Brief. Bioinformatics 5 (2004) 150–163.[25] M. Biasini, S. Bienert, A. Waterhouse, K. Arnold, G. Studer, T. Schmidt, F. Kiefer, T. G. Cassarino, M. Bertoni, L. Bordoli, SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information, Nucleic Acids Res. 42 (2014) W252–W258.[26] D. Case, T. Darden, T. Cheatham III, C. Simmerling, J. Wang, R. Duke, R. Luo, R. Walker, W. Zhang, K. Merz, AMBER 12, University of California, San Francisco, 2010, pp. 1–826, 2012, There is no corresponding record for this reference.[Google Scholar].[27] R.L. Tellam, Protein motifs in filarial chitinases: an alter-native view, Parasitol. Today 12 (1996) 291–292.[28] Q. Zhu, Y. Deng, P. Vanka, S.J. Brown, S. Muthukrishnan, K.J. Kramer, Computational identification of novel chitinase-like proteins in the Drosophila melanogaster genome, Bioinformatics 20 (2004) 161–169.[29] Z. Shen, M. Jacobs-Lorena, Evolution of chitin-binding proteins in invertebrates, J. Mol. Evol. 48 (1999) 341–347.[30] Y. Arakane, Q. Zhu, M. Matsumiya, S. Muthukrishnan, K.J. Kramer, Properties of catalytic, linker and chitin-binding domains of insect chitinase, Insect Biochem. Mol. Biol. 33 (2003) 631–648.[31] M. Quentin, M. Ebbelaar, J. Derksen, C. Mariani, H. van Der Valk, Description of a cellulose-binding domain and a linker sequence from Aspergillus fungi, Appl. Microbiol. Biotechnol. 58 (2002) 658–662.[32] M. Rechsteiner, S.W. Rogers, PEST sequences and regulation by proteolysis, Trends Biochem. Sci. 21 (1996) 267–271.[33] R. Sotelo-Mundo, E. Moran-Palacio, K. García-Orozco, C. Figueroa-Soto, M. Romo-´ Figueroa, E. Valenzuela-Soto, G. Yepiz-Plascencia, Kinetic characterization, expression and molecular modeling of a chitinase from the pacific white shrimp Litopenaeus vannamei, J. Food Biochem. 33 (2009) 246–259.[34] M. Kono, T. Matsui, C. Shimizu, D. Koga, Purifications and some properties of chitinase from the liver of a prawn, Penaeus japonicus, Agric. Biol. Chem. 54 (1990) 2145–2147.[35] X.-L. Xie, Q.-X. Chen, J.-C. Lin, Y. Wang, Purification and some properties of β-N- acetyl-D-glucosaminidase from prawn (Penaeus vannamei), Mar. Biol. 146 (2004) 143–148.[36] D. Koga, K. Mizuki, A. Ide, M. Kono, T. Matsui, C. Shimizu, Kinetics of a chitinase from a prawn, Penaeus japonicus, Agric. Biol. Chem. 54 (1990) 2505–2512.[37] F. Shojaei, A. Homaei, M.R. Taherizadeh, E. 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Identification of a novel tailor-made chitinase from white shrimp fenneropenaeus merguiensis

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