Cross‐Linking of Myosin Heavy Chains from Cod, Herring and Silver Hake During Thermal Setting
ABSTRACT 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‐...
| Published in: | Journal of Food Science |
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| Main Authors: | , , |
| Format: | Article in Journal/Newspaper |
| Language: | English |
| Published: |
Wiley
1992
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| Subjects: | |
| Online Access: | http://dx.doi.org/10.1111/j.1365-2621.1992.tb14320.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1365-2621.1992.tb14320.x http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1365-2621.1992.tb14320.x/fullpdf |
| Summary: | ABSTRACT 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). |
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