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Cross‐Linking of Myosin Heavy Chains from Cod, Herring and Silver Hake During Thermal Setting
Author(s) -
CHAN J.K.,
GILL T.A.,
PAULSON AT.
Publication year - 1992
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.1365-2621.1992.tb14320.x
Subject(s) - hake , clupea , myosin , merluccius , herring , chemistry , gadus , myofibril , fishery , merluccius merluccius , food science , biochemistry , fish <actinopterygii> , biology
Cross‐linking of myofibrillar proteins extracted from cod ( Gadus morhua) , herring ( Clupea harengus ) and silver hake ( Merluccius bilinearis ) was studied in 0.6M NaCl, pH 6.5 at 40°C and evaluated turbidimetrically and by SDS polyacrylamide gel electrophoresis coupled with l‐ethyl‐3‐(3‐dimethylaminopropyl) carbodiimide as a zero‐length crosslinker. Turbidities of heat‐treated cod and silver hake myofibril/myosin solutions were significantly higher than those of herring. Electrophoretic results showed that the myosin heavy chain (MHC) was the principal myofibrillar protein cross‐linked to form a polymerized complex during the heat treatment. Cross‐linking ability of MHC from the three fish species was different; herring MHC formed only small polymers (n≦3) but cod and silver hake MHC formed both small and large polymers (n≦6).