Metal-sensitive and thermostable trypsin from the crevalle jack (Caranx hippos) pyloric caeca: purification and characterization

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dc.contributor.authorCosta, Helane M. S.
dc.contributor.authorFreitas Junior, Augusto C. V.
dc.contributor.authorAmaral, Ian P. G.
dc.contributor.authorHirata, Izaura Y. [UNIFESP]
dc.contributor.authorPaiva, Patricia M. G.
dc.contributor.authorCarvalho, Luiz B.
dc.contributor.authorOliveira, Vitor [UNIFESP]
dc.contributor.authorBezerra, Ranilson S.
dc.contributor.institutionUniversidade Federal de Pernambuco (UFPE)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2016-01-24T14:34:35Z
dc.date.available2016-01-24T14:34:35Z
dc.date.issued2013-10-10
dc.description.abstractBackground: Over the past decades, the economic development and world population growth has led to increased for food demand. Increasing the fish production is considered one of the alternatives to meet the increased food demand, but the processing of fish leads to by-products such as skin, bones and viscera, a source of environmental contamination. Fish viscera have been reported as an important source of digestive proteases with interesting characteristics for biotechnological processes. Thus, the aim of this study was to purify and to characterize a trypsin from the processing by-products of crevalle jack (Caranx hippos) fish.Results: A 27.5 kDa trypsin with N-terminal amino acid sequence IVGGFECTPHVFAYQ was easily purified from the pyloric caeca of the crevalle jack. Its physicochemical and kinetic properties were evaluated using N-alpha-benzoyl-(DL)-arginine-p-nitroanilide (BApNA) as substrate. in addition, the effects of various metal ions and specific protease inhibitors on trypsin activity were determined. Optimum pH and temperature were 8.0 and 50 degrees C, respectively. After incubation at 50 degrees C for 30 min the enzyme lost only 20% of its activity. K-m, k(cat), and k(cat)/K-m values using BApNA as substrate were 0.689 mM, 6.9 s(-1), and 10 s(-1) mM(-1), respectively. High inhibition of trypsin activity was observed after incubation with Cd2+, Al3+, Zn2+, Cu2+, Pb2+, and Hg2+ at 1 mM, revealing high sensitivity of the enzyme to metal ions.Conclusions: Extraction of a thermostable trypsin from by-products of the fishery industry confirms the potential of these materials as an alternative source of these biomolecules. Furthermore, the results suggest that this trypsin-like enzyme presents interesting biotechnological properties for industrial applications.en
dc.description.affiliationUniv Fed Pernambuco, Lab Enzimol LABENZ, Dept Bioquim CCB, BR-50670910 Recife, PE, Brazil
dc.description.affiliationUniv Fed Pernambuco, LIKA, BR-50670910 Recife, PE, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biofis, Escola Paulista Med, BR-04044020 São Paulo, Brazil
dc.description.affiliationUniv Fed Pernambuco, Lab Glicoprot, Dept Bioquim CCB, BR-50670910 Recife, PE, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biofis, Escola Paulista Med, BR-04044020 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipFinanciadora de Estudos e Projetos (FINEP/RECARCINE)
dc.description.sponsorshipPetroleo do Brasil S/A (PETROBRAS)
dc.description.sponsorshipSecretaria Especial de Aquicultura e Pesca (SEAP/PR)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipFundacao de Apoio a Ciencia e Tecnologia do Estado de Pernambuco (FACEPE)
dc.format.extent8
dc.identifierhttp://dx.doi.org/10.1186/1752-153X-7-166
dc.identifier.citationChemistry Central Journal. London: Biomed Central Ltd, v. 7, 8 p., 2013.
dc.identifier.doi10.1186/1752-153X-7-166
dc.identifier.fileWOS000327602500002.pdf
dc.identifier.issn1752-153X
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/36874
dc.identifier.wosWOS:000327602500002
dc.language.isoeng
dc.publisherBiomed Central Ltd
dc.relation.ispartofChemistry Central Journal
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectCaranx hipposen
dc.subjectCrevalle jacken
dc.subjectFish trypsinen
dc.subjectMarine fishen
dc.subjectN-terminal amino acid sequenceen
dc.subjectThermostable trypsinen
dc.subjectWaste recoveryen
dc.titleMetal-sensitive and thermostable trypsin from the crevalle jack (Caranx hippos) pyloric caeca: purification and characterizationen
dc.typeinfo:eu-repo/semantics/article
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