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Proteinase in Pacific Whiting Surimi Wash Water: Identification and Characterization
Author(s) -
BENJAKUL SOOTTAWAT,
SEYMOUR THOMAS A.,
MORRISSEY MICHAEL T.,
AN HAEJUNG
Publication year - 1996
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1996.tb10953.x
Subject(s) - whiting , chemistry , cathepsin , substrate (aquarium) , chromatography , cathepsin l , size exclusion chromatography , cathepsin b , molecular mass , biochemistry , enzyme , fishery , fish <actinopterygii> , biology , ecology
A proteinase in Pacific whiting surimi wash water (SWW) was characterized to be cathepsin L based on molecular mass (M r ), substrate specificity, and SDS‐substrate gel electrophoresis. The proteinase was highly active on Z‐Phe‐Arg‐NMec, and the native M r was 27,400 based on size exclusion (SEC)‐HPLC. Acidification of the SEC‐HPLC fractions showed a two‐fold increase in activity on Z‐Phe‐Arg‐NMec. SWW proteolytic activity was found at M r 54,200 on SDS‐substrate gel. However, acidification shifted the activity zone to M r 39,500 corresponding to cathepsin L. No evidence of activity by calpain or cathepsin B or H was found in Pacific whiting SWW.