The effect of freezing and aldehydes on the interaction between fish myoglobin and myofibrillar proteins |
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Authors: | Chaijan Manat Benjakul Soottawat Visessanguan Wonnop Lee Seok Faustman Cameron |
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Institution: | Department of Food Technology, Faculty of Agro-Industry, Prince of Songkla University, Hat Yai, 90112, Thailand. |
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Abstract: | The interaction between fish myoglobin (Mb) and natural actomyosin (NAM) extracted from fresh and frozen fish was studied. The quantity of soluble Mb in Mb-NAM extracted was less in frozen than in fresh fish (P < 0.05). However, no differences were observed in Mb that remained in solution following preparation of Mb-NAM from frozen whole fish vs frozen fillets (P > 0.05). MetMb formation in Mb-NAM was generally greater than that observed in control Mb (P < 0.05); the greatest MetMb content occurred in Mb-NAM extracted from frozen whole fish (P < 0.05). The effect of different aldehyde oxidation products on the interaction between fish Mb and NAM was also studied in vitro. The loss of soluble Mb from NAM:Mb preparations was greater in the presence of hexenal and hexanal (P < 0.05) relative to controls, and the degree of solubility loss varied with aldehyde type. Hexenal caused greater OxyMb oxidation than hexanal (P < 0.05). Whiteness of washed NAM and NAM-Mb mixtures decreased following aldehyde addition (P < 0.05). In the absence of Mb, the Ca2+ -ATPase activity of NAM was lower with added hexenal than with hexanal (P < 0.05). However, no differences in Ca2+ -ATPase activity between hexanal and hexenal-treated samples were observed when Mb was present (P > 0.05). Reducing and nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis analyses suggested that both disulfide and nondisulfide covalent linkages contributed to aldehyde-induced cross-linking between Mb and myofibrillar proteins. |
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