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

dc.creatorBeygmoradi, Azadeh
dc.creatorHomaei, Ahmad
dc.creatorHemmati, Roohullah
dc.creatorDel Arco, Jon
dc.creatorFernández-Lucas, Jesús
dc.date2021-05-04T23:30:55Z
dc.date2021-05-04T23:30:55Z
dc.date2021
dc.date2023
dc.date.accessioned2023-10-03T20:11:54Z
dc.date.available2023-10-03T20:11:54Z
dc.identifier0927-7765
dc.identifier1873-4367
dc.identifierhttps://hdl.handle.net/11323/8221
dc.identifierhttps://doi.org/10.1016/j.colsurfb.2021.111747
dc.identifierCorporación Universidad de la Costa
dc.identifierREDICUC - Repositorio CUC
dc.identifierhttps://repositorio.cuc.edu.co/
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/9174743
dc.descriptionFenneropenaeus 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.
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dc.languageeng
dc.publisherCorporación Universidad de la Costa
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dc.rightsCC0 1.0 Universal
dc.rightshttp://creativecommons.org/publicdomain/zero/1.0/
dc.rightsinfo:eu-repo/semantics/openAccess
dc.rightshttp://purl.org/coar/access_right/c_abf2
dc.sourceColloids and Surfaces B: Biointerfaces
dc.sourcehttps://www.sciencedirect.com/science/article/pii/S0927776521001910?via%3Dihub
dc.subjectMarine organisms
dc.subjectChitinolitic enzymes
dc.subjectMolecular cloning
dc.subjectProtein purification
dc.subjectBiochemical characterization
dc.titleIdentification of a novel tailor-made chitinase from white shrimp fenneropenaeus merguiensis
dc.typePre-Publicación
dc.typehttp://purl.org/coar/resource_type/c_816b
dc.typeText
dc.typeinfo:eu-repo/semantics/preprint
dc.typeinfo:eu-repo/semantics/draft
dc.typehttp://purl.org/redcol/resource_type/ARTOTR
dc.typeinfo:eu-repo/semantics/acceptedVersion
dc.typehttp://purl.org/coar/version/c_ab4af688f83e57aa


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