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Mackerel Cathepsins B and L Effects on Thermal Degradation of Surimi
Author(s) -
JIANG SHANNTZONG,
LEE BAILIN,
TSAO CHINGYU,
LEE JAIJAAN
Publication year - 1997
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.1365-2621.1997.tb03991.x
Subject(s) - chemistry , cathepsin , cathepsin b , hydrolysis , food science , biochemistry , cathepsin l , myosin , enzyme
ABSTRACT During surimi processing, cathepsins B and L activities in minced, leached and NaCl‐ground meats were 6.02, 5.23, and 4.07 units/g, respectively. About 80% activity remained in surimi after 8 wk storage at −40°C suggesting that these proteinases were stable and difficult to remove. At 40°∼ 55°C, pH 6.5 ∼ 7.5, cathepsins B and L and purified cathepsin B had high hydrolytic activity on myosin heavy chain (MHC). The strength of surimi gel with cathepsins B and L or with purified B decreased (p < 0.05) after 2 hr incubation at 55°C. This suggested that the residual cathepsins B and L had MHC‐degrading activity and consequently caused gel softening.