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Purification and partial characterisation of a trypsin from the processing waste of the silver mojarra (Diapterus rhombeus) by Janilson F. Silva; Talita S. Espósito; Marina Marcuschi; Karina Ribeiro; Ronaldo O. Cavalli; Vitor Oliveira; Ranilson S. Bezerra is a Agricultural and Biological Sciences article available to read on EtoBox.

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An alkaline peptidase was purified from the viscera of the silver mojarra (Diapterus rhombeus) in a threestep process: heat treatment, ammonium sulphate fractionation and molecular exclusion chromatography (Sephadex Ò G-75), with final specific activity 86-fold higher than the enzyme extract and yield of 22.1%. The purified enzyme had an estimated molecular mass of 26.5 kDa and NH 2 -terminal amino acid sequence IVGGYECTMHSEAHE. Higher enzyme activity was observed at pH 8.5 and between 50 and 55 °C. The enzyme was completely inactivated after 30 min at 55 °C and it was significantly more stable at alkaline pH. K m , K cat and K cat Á K À1 m values, using BApNA as substrate, were 0.266 mM, 0.93 s À1 and 3.48 mM À1 s À1 , respectively. Enzyme activity increased in the presence of the ions (1 mM) K + , Li + and Ca 2+ , but was inhibited by Fe 2+ , Cd 2+ , Cu 2+ , Al 3+ , Hg 2+ , Zn 2+ and Pb 2+ as well as by the trypsin inhibitors TLCK and benzamidine.

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Author

Janilson F. Silva; Talita S. Espósito; Marina Marcuschi; Karina Ribeiro; Ronaldo O. Cavalli; Vitor Oliveira; Ranilson S. Bezerra

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 0308-8146)

Published

2011

Language

EN

Field

Agricultural and Biological Sciences (Life Sciences)