Determination of hydrophobicity and reactive groups in proteins of cod (Gadus morhua) muscle during frozen storage
1992
LeBlanc, E.L. | LeBlanc, R.J.
This study, to elucidate the possible sources of protein denaturation and cross-linkage which cause textural deterioration, was a continuation of our work on the same lot of commercially harvested and processed fillets of Northern bank trawl cod (Gadus morhua), frozen stored for ca. 300 days at -30 degrees C, -22 degrees C, -15 degrees C, -12 degrees C and under conditions of fluctuating temperatures simulating industrial practice. Sarcoplasmic, myosin-rich and SDS-soluble protein fractions from each treatment were evaluated for surface hydrophobicity, total, available and unavailable SH-, SS-, aldehydes, free NH2- and ester-link content. Changes in surface hydrophobicity in the three fractions may be caused by increases in SS- bonding, ester-links, aldehydes and free NH2- groups. These results demonstrate that hydrophobicity is not only attributed to SS- formation but also to ester-links, aldehydes and free NH2- groups.
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