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Effect of soluble soybean polysaccharides on freeze-denaturation and structure of myofibrillar protein of bighead carp surimi with liquid nitrogen freezing
- Gao, Wenhong, Huang, Yangping, Zeng, Xin-an, Brennan, Margaret A.
- International journal of biological macromolecules 2019 v.135 pp. 839-844
- Ca2-transporting ATPase, Hypophthalmichthys nobilis, Raman spectroscopy, disulfide bonds, enzyme activity, freezing, frozen storage, liquids, myosin heavy chains, nitrogen, polyacrylamide gel electrophoresis, polysaccharides, protein denaturation, protein solubility, soybeans, surimi, synergism, tryptophan, tyrosine
- This paper investigated the synergistic effect of 3% soluble soybean polysaccharides (SSPS) and liquid nitrogen freezing (−80 °C) on the freezing process and protein denaturation of bighead carp surimi. Freezing curve showed that liquid nitrogen freezing could significantly minimize the elapsed time of maximum-ice-crystal formation zone. Both liquid nitrogen freezing and SSPS were useful in preventing protein denaturation of surimi during 12-week frozen storage. Protein denaturation results indicated that SSPS-LNfreezing surimi11SSPS-added surimi frozen by liquid nitrogen freezing had the highest protein solubility, Ca2+-ATPase activity and total sulfhydryl content. SDS-PAGE indicated that SSPS and liquid nitrogen freezing could effectively inhibit the decrease of myosin heavy chain concentration after 12 weeks of frozen storage. Raman spectra showed that tryptophan and tyrosine were exposed to polar microenvironment, the ɑ-helix and β-sheet turned into random coil and β-turn, and the conformation of disulfide bond changed from trans-gauche-trans (t-g-t) to gauche-gauche-trans (g-g-t). Either SSPS or liquid nitrogen freezing could mitigate these changes during frozen storage and a synergistic effect emerged on preventing myofibrillar protein denaturation and protein structure change. The combination of SSPS with liquid nitrogen freezing could be applied to freeze bighead carp surimi.