Frozen storage of minced Greenland halibut (Reinhardtius hippoglossoides) at ‐10°C resulted in a rapid loss in salt solubility of “my ofibrillar proteins” (approximately 50% in 15 days) and in a gradual loss in water solubility of “sarcoplasmic proteins” (approximately 40% in 120 days). The water and salt inextractable protein from frozen mince (R) was completely soluble in 4% sodium dodecylsulfate (SDS) when a disulfide bond reducing agent such as mercaptoethanol (ME) was present. Other reagents, including urea and Triton X 100, were less effective in solubilizing the protein from mince after frozen storage. Evidence presented supports the thesis that disulfide bond formation contributes to the observed loss in protein extractability during frozen storage of mince. Addition of various thiol reagents to mince prior to freezing was effective in minimizing protein insolubilization. An estimated 50% of the reduced cysteine associated with protein is oxidized in mince after long time storage at ‐10°C. However, the kinetics of disulfide bond formation do not parallel the time course of protein insolubilization; accordingly, the possibility that disulfide bond formation is a secondary event cannot be excluded. Other lines of evidence indicate that additional covalent or strong bond interactions contribute to the formation of(R). Solubilization and boiling of(R) in SDS/ME does not dissociate high molecular weight aggregates (500–1000 Kdaltons) although these aggregates are disrupted by sodium borohydride reduction. In addition, the degree of hydrolysis of proteins in frozen mince by certain proteolytic enzymes is lower then that of fresh mince despite the complete solubilization of the mince protein by these proteolytic enzymes. The mince protein from frozen fish contains substantially more fluorescence than that of fresh fish. Fluorescence is associated with the high molecular weight peptide fraction after pepsin catalyzed hydrolysis. The amino acid composition of mince proteins after HCl or formic acid/HCl hydrolysis did not change appreciably as a result of frozen storage. The data indicate that covalent bond formation by sulfhydryl residues and other borohydride and acid labile linkages contribute to the loss in solubility of the protein in Greenland halibut mince during frozen storage at ‐10°C.
Journal of Food Biochemistry – Wiley
Published: Sep 1, 1984
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