Premium
Effect of protease inhibitors on proteolytic degradation of rohu ( Labeo rohita ) gel
Author(s) -
Sutloet Phatthira,
Sompongse Warangkana,
Morioka Katsuji
Publication year - 2018
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/ijfs.13844
Subject(s) - leupeptin , autolysis (biology) , protease , proteases , trypsin , biochemistry , protease inhibitor (pharmacology) , kunitz sti protease inhibitor , chemistry , biology , microbiology and biotechnology , enzyme , virus , virology , antiretroviral therapy , viral load
Summary Endogenous proteases are responsible for gel weakening of fish muscle protein. We investigated inhibitory effect of four selected protease inhibitors: soya bean trypsin inhibitor, leupeptin, E64 and EDTA , to identify the protease groups responsible for gel degradation in both unwashed and washed rohu ( Labeo rohita ) gel. The protease inhibitory activity was determined by percentage inhibition and SDS ‐ PAGE pattern. Leupeptin and E64 showed a strong inhibition on the autolysis of unwashed gel, and myosin heavy chain ( MHC ) band was recovered by the addition of them. The results suggested that cysteine protease was the major endogenous protease involved in the autolysis. In the case of the washed gel, leupeptin and soya bean trypsin inhibitor were shown to have a strong inhibitory effect. Also, the addition of these inhibitors increased the intensity of the MHC band. The results implied that serine protease played an important role in the degradation of the gel network.