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- W2525058783 abstract "Enzyme extracts obtained from I. fuscus ventral muscle were studied. Peak activity was observed at pH 2, 6, and 8, and 50-60°C, whereas maximum enzymatic stability occurred at pH 2 to 6 (except pH 3) and 0 to 40°C. More than 74% residual activity was retained after heating at 70°C and 80°C for 1 h, confirming the presence of heat-resistant enzymes. The extracts also retained 59% initial activity after 21-day storage at 4-5°C. Hg 2+ increased the proteolytic activity in 16%, whereas Cu 2+ and Mn 2+ caused partial inhibition, suggesting the presence of cysteine- and metallo- proteases. Extracts were inhibited by pepstatin A, -mercaptoethanol and EDTA, confirming the predominance of aspartyl-, cystein-, and metallo-, proteases. Four proteins were identified by SDS-PAGE (180.6, 114.5, 91.7 and 52.9 kDa). Zymograms on casein confirmed the presence of proteolytic enzymes. After purification by anion exchange chromatography a 49 kDa protease, possible metalloprotease, was detected. Mass spectrometry of the partially purified protein showed homology with trypsin and chain E, leech-derived tryptase inhibitor trypsin complex (LDTI). Due that no homology was found with any previously described metalloproteases, the presence of a novel enzyme is suggested." @default.
- W2525058783 created "2016-10-07" @default.
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- W2525058783 date "2015-01-01" @default.
- W2525058783 modified "2023-09-23" @default.
- W2525058783 title "ON Y CARACTERIZACI ´ ON DE PROTEASAS DE PEPINO DE MAR Isostichopus fuscus RECOLECTADO EN EL GOLFO DE CALIFORNIA, M ´ EXICO EXTRACTION AND CHARACTERIZATION OF SEA CUCUMBER Isostichopus fuscus PROTEASES, COLLECTED AT THE GULF OF CALIFORNIA, MEXICO" @default.
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