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Heat induced changes in sulfhydryl groups and di sulfide bonds in fish protein and their effect on protein and amino acid digestibility in rainbow trout salmo gairdneri


, : Heat induced changes in sulfhydryl groups and di sulfide bonds in fish protein and their effect on protein and amino acid digestibility in rainbow trout salmo gairdneri. Journal of Agricultural & Food Chemistry 32(4): 929-935

Ground fillets of frozen Alaska pollock (Theragra chalcogramma), a low-fat fish, and Pacific mackerel (Pneumataphorus japanicus), a high-fat fish, heated for 20 min at temperature intervals ranging from 40.degree.-115.degree. C showed a linear decrease in the content of SH groups and a concomitant increase in the content of S.sbd.S (disulfide) bonds from 50.degree.-115.degree. C. At 95.degree. C, the reaction was rapid and reached an equilibrium after 20 min. Temperatures > 50.degree. C are thus required for oxidative transformation of SH groups to S.sbd.S bonds. Heating at 115.degree. C caused a loss in cystine plus cysteine. Heating to 95.degree. C and drum-drying caused the formation of S.sbd.S bonds from SH groups and reduced protein and amino acid digestibility when fed to rainbow trout (S. gairdneri) as compared with the raw fish protein. Freeze-drying did not affect digestibility and no formation of S.sbd.S bonds was found. Heat-induced S.sbd.S cross-linking from SH oxidation apparently causes a reduction in protein and amino acid digestibility in drum-dried samples. The effect of heating on digestibility was greater in the low-fat pollock than in the high-fat mackerel.

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