Hydrolysis of surimi paste from walleye pollock ( Theragra chalcogramma) by cysteine proteinase cathepsin L and effect of the proteinase inhibitor (E-64) on gelation

The gel strength of kamaboko obtained from walleye pollock ( Theragra chalcogramma) was much reduced when the surimi paste was incubated at 60 °C for 2 h. The proteinase inhibitor, E-64, could enhance the gel strength and, at 200 μg/g of surimi, appeared to be the most effective. Amino acid analysis...

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Bibliographic Details
Published in:Food chemistry 2007, Vol.104 (2), p.702-708
Main Authors: Hu, Yaqin, Morioka, Katsuji, Itoh, Yoshiaki
Format: Article
Language:English
Subjects:
Biological and medical sciences
Cathepsin L
cathepsins
Cysteine protease
cysteine proteinases
E-64
enzymatic hydrolysis
enzyme activity
enzyme substrates
fish paste
Food industries
Fundamental and applied biological sciences. Psychology
Gel strength
gelation
Hydrolysis
kamaboko
modori phenomena
proteinase inhibitors
substrate specificity
surimi
texture
Theragra chalcogramma
Walleye pollock surimi
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Summary:The gel strength of kamaboko obtained from walleye pollock ( Theragra chalcogramma) was much reduced when the surimi paste was incubated at 60 °C for 2 h. The proteinase inhibitor, E-64, could enhance the gel strength and, at 200 μg/g of surimi, appeared to be the most effective. Amino acid analysis of the corresponding kamaboko showed that E-64 suppressed the release of peptides. Electrophoretograms revealed the inhibition of MHC degradation by E-64. Actomyosin was extracted and subjected to Sepharose 6B gel filtration to obtain the actomyosin non-binding cathepsin L (L mix). Studies of substrate specificity and the effect of activators and inhibitors confirmed that the thiol–cysteine enzyme obtained was crude cathepsin L. Its high heat-stability indicated its strong hydrolytic ability. L mix, at 0.6 unit/g of surimi, greatly decreased walleye pollock kamaboko gel strength from 112 to 27.8 g/cm 2 when incubated at 60 °C for 2 h. The degradation was effectively inhibited by E-64 at 200 μg/g of surimi and the gel strength of the corresponding kamaboko was increased to 302 g/cm 2. The above results suggested that cathepsin L contributed to the modori phenomena in kamaboko processed from walleye pollock surimi.
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2006.12.032