Journal
FOOD CHEMISTRY
Volume 110, Issue 2, Pages 310-318Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2008.01.068
Keywords
cathepsin B; silver carp; purification; surimi; gel softening
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Cathepsin B from silver carp muscle was purified to 263-fold by acid treatment, ammonium sulfate fractionation, followed by a series of chromatographic separations. The molecular mass of the purified enzyme was 29 kDa as determined by SDS-PAGE and immunoblotting. The purified enzyme was activated by dithiothreitol and cysteine while it was substantially inhibited by E-64, suggesting the purified enzyme belongs to the cysteine proteinase family. Optimal pH and temperature were 5.5 and 35 degrees C, respectively. The enzyme catalyzed the hydrolysis of Z-Arg-Arg-MCA with a parameter of K-m (90 mu M) and K-cat (20.3 s(-1)), but hardly hydrolyzed Arg-MCA. Analysis of surimi gel strength and microstructure showed that cathepsins B and L were capable of destroying the network structure of silver carp surimi gels, consequently causing gel softening. Cathepsin L might play an important role in the modori effect. (c) 2008 Elsevier Ltd. All rights reserved.
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