Proteases from the Harpacticoid Copepod Tisbe biminiensis: Comparative Study with Enzymes from Farmed Aquatic Animals
Identifieur interne : 000824 ( Main/Merge ); précédent : 000823; suivant : 000825Proteases from the Harpacticoid Copepod Tisbe biminiensis: Comparative Study with Enzymes from Farmed Aquatic Animals
Auteurs : Renata C. P. Frana [Brésil] ; Ian P. G. Amaral ; Werlayne M. Santana ; Llia P. Souza-Santos [Brésil] ; Luiz B. Carvalho ; Ranilson S. Bezerra [Brésil]Source :
- Journal of Crustacean Biology [ 0278-0372 ] ; 2010-02.
Abstract
The harpacticoid copepod Tisbe biminiensis has been tested as live prey in marine crustacean and fish larviculture. The aim of the present study was to characterize the proteinases in the crude extract of T. biminiensis. Trypsin activity was assayed in the crude extract prepared by the homogenization of specimens reared under controlled laboratory conditions and fed on diatoms and commercial fish food. The physical-chemical and kinectics parameters were determined using BApNA as substrate. Optimal pH and temperature were 9.0 and 55C, respectively. This enzyme was thermostable until 50C. Using BApNA as substrate, the Km was 0.59 mM and the proteolytic activity was strongly inhibited by specific trypsin inhibitors. However, the presence of other proteases was observed using substrate-SDS-PAGE. Eight caseinolytic bands were observed in the zymogram, four of them were not inhibited by classical mammalian trypsin inhibitors. Trypsin from T. biminiensis showed similar properties to those described for species used in commercial aquaculture. These results demonstrate that T. biminiensis may be a source of proteases, including trypsin-like enzymes.
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DOI: 10.1651/08-3127.1
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Bezerra</name><affiliation wicri:level="2"><country xml:lang="fr">Brésil</country><wicri:regionArea>Laboratrio de Enzimologia, Departamento de Bioqumica and Laboratrio de Imunopatologia Keizo Asami (LIKA), Universidade Federal de Pernambuco, Cidade Universitaria, 50670-420, Recife-PE</wicri:regionArea><placeName><region type="state">Pernambuco</region></placeName></affiliation><affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Crustacean Biology</title><title level="j" type="abbrev">JCB</title><idno type="ISSN">0278-0372</idno><idno type="eISSN">1937-240X</idno><imprint><publisher>VSP</publisher><pubPlace>Netherlands</pubPlace><date type="published" when="2010-02">2010-02</date><biblScope unit="volume">30</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="122">122</biblScope><biblScope unit="page" to="128">128</biblScope></imprint><idno type="ISSN">0278-0372</idno></series><idno type="istex">3094E25F690FE1E13EDB55B3F1E4DA9215AF8D32</idno><idno type="DOI">10.1651/08-3127.1</idno><idno type="ArticleID">08-3127</idno><idno type="pdf">08-3127.1.pdf</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0278-0372</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The harpacticoid copepod Tisbe biminiensis has been tested as live prey in marine crustacean and fish larviculture. The aim of the present study was to characterize the proteinases in the crude extract of T. biminiensis. Trypsin activity was assayed in the crude extract prepared by the homogenization of specimens reared under controlled laboratory conditions and fed on diatoms and commercial fish food. The physical-chemical and kinectics parameters were determined using BApNA as substrate. Optimal pH and temperature were 9.0 and 55C, respectively. This enzyme was thermostable until 50C. Using BApNA as substrate, the Km was 0.59 mM and the proteolytic activity was strongly inhibited by specific trypsin inhibitors. However, the presence of other proteases was observed using substrate-SDS-PAGE. Eight caseinolytic bands were observed in the zymogram, four of them were not inhibited by classical mammalian trypsin inhibitors. Trypsin from T. biminiensis showed similar properties to those described for species used in commercial aquaculture. These results demonstrate that T. biminiensis may be a source of proteases, including trypsin-like enzymes.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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