Cross‐Linking of Myosin Heavy Chains from Cod, Herring and Silver Hake During Thermal Setting

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Published
1992-07
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  • http://onlinelibrary.wiley.com/termsAndConditions#vor
DOI
  • 10.1111/j.1365-2621.1992.tb14320.x
Publisher
Wiley

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<jats:title>ABSTRACT</jats:title> <jats:p> Cross‐linking of myofibrillar proteins extracted from cod ( <jats:italic>Gadus morhua)</jats:italic> , herring ( <jats:italic>Clupea harengus</jats:italic> ) and silver hake ( <jats:italic>Merluccius bilinearis</jats:italic> ) 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). </jats:p>

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