TRYPSIN FROM JUMBO SQUID (Dosidicus gigas) HEPATOPANCREAS: PURIFICATION AND CHARACTERIZATION

Trypsin was purified from the hepatopancreas of Dosidicus gigas by f ractionation with ammonium sulfate (30-70% saturation), gel filtration, affinity and ion exchange chromatography. The molecular weight of the trypsin obtained was ~23.5kDa according to sodium dodecyl sulfate-polyacrylamide gel elec...

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Detalles Bibliográficos
Autores: Ana Gloria Villalba-Villalba, Enrique Márquez-Ríos, Marina Josafat Esquerra- Brauer, Francisco Javier Castillo-Yáñez
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2017
País:México
Institución:Universidad de Sonora
Repositorio:Redalyc-USON
OAI Identifier:oai:redalyc.org:33950011005
Acceso en línea:https://www.redalyc.org/articulo.oa?id=33950011005
https://www.redalyc.org/journal/339/33950011005/
https://www.redalyc.org/journal/339/33950011005/html/
https://www.redalyc.org/journal/339/33950011005/33950011005.epub
https://www.redalyc.org/journal/339/33950011005/movil
Access Level:acceso abierto
Palabra clave:Multidisciplinarias (Ciencias Sociales)
Squid
Trypsin
Hepatopancreas
Dosidicus gigas
Enzyme Purification
Descripción
Sumario:Trypsin was purified from the hepatopancreas of Dosidicus gigas by f ractionation with ammonium sulfate (30-70% saturation), gel filtration, affinity and ion exchange chromatography. The molecular weight of the trypsin obtained was ~23.5kDa according to sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and, showed a single band in the zymogram. The enzyme exhibited maximal activity at pH 8.5 and 40ºC, using BAPNA as substrate. It was effectively inhibited by phenyl methyl sulfonyl fluoride (PMSF) (98%), and Nα-p-Tosyl-L-lysine chloromethyl ketone (TLCK) (99%). Enzyme activity was affected by the following ions in decreasing order: Hg2+, Fe2+, Cu2+, Li1+, Mg2+, K1+, Mn2+, Ca2+. Trypsin activity decreased continuously as NaCl concentration increased from 0 to 30%. Km and kcat values were 0.085 ±1.45mM and 1.76 ±0.12s-1, respectively. The results suggest that the purified enzyme a potential agent to be used in biotechnological processes.