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Proteolytic Degradation of Tropical Tilapia Surimi
Author(s) -
Yongsawatdigul J.,
Park J.W.,
Virulhakul P.,
Viratchakul S.
Publication year - 2000
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.1365-2621.2000.tb15967.x
Subject(s) - proteolysis , tilapia , leupeptin , myosin , chemistry , trypsin , biochemistry , proteases , protease , degradation (telecommunications) , food science , biology , fish <actinopterygii> , enzyme , fishery , telecommunications , computer science
Proteolytic degradation of tropical tilapia surimi was biochemically and rheologically characterized to identify a group of proteinase(s) responsible for its textural degradation. Proteolysis of tilapia surimi occurred as the temperature increased and attained the highest activity at 65 °C. Smaller proteins with molecular weight of 116‐97 kDa were noted as a result of myosin heavy chain (MHC) degradation. MHC completely disappeared when incubated at 65 °C for 4 h. Proteolysis was significantly inhibited by soybean trypsin inhibitor (SB) and leupeptin (LE). Storage modulus (G′) of surimi gels mixed with either SB or LE was higher than other inhibitors indicating that serine type proteinase(s) were involved in proteolysis of tropical tilapia surimi.