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中国精品科技期刊2020
高宇, 毕保良, 贾丹, 胡青, 王晓雯. 青鱼和鲢鱼肌球蛋白热诱导凝胶特性的比较[J]. 食品工业科技, 2021, 42(3): 1-5,12. DOI: 10.13386/j.issn1002-0306.2020030335
引用本文: 高宇, 毕保良, 贾丹, 胡青, 王晓雯. 青鱼和鲢鱼肌球蛋白热诱导凝胶特性的比较[J]. 食品工业科技, 2021, 42(3): 1-5,12. DOI: 10.13386/j.issn1002-0306.2020030335
GAO Yu, BI Baoliang, JIA Dan, HU Qing, WANG Xiaowen. Comparison of the Properties of Heat-induced Gel of Black Carp and Silver Carp Myosin[J]. Science and Technology of Food Industry, 2021, 42(3): 1-5,12. DOI: 10.13386/j.issn1002-0306.2020030335
Citation: GAO Yu, BI Baoliang, JIA Dan, HU Qing, WANG Xiaowen. Comparison of the Properties of Heat-induced Gel of Black Carp and Silver Carp Myosin[J]. Science and Technology of Food Industry, 2021, 42(3): 1-5,12. DOI: 10.13386/j.issn1002-0306.2020030335

青鱼和鲢鱼肌球蛋白热诱导凝胶特性的比较

Comparison of the Properties of Heat-induced Gel of Black Carp and Silver Carp Myosin

  • 摘要: 以青鱼(Mylopharyngodon piceus)和鲢鱼(Hypophthalmichthys molitrix)为研究对象,通过测定肌球蛋白在热诱导凝胶形成过程中的二级结构、表面疏水性(S0-ANS)、二硫键、平均粒径(dz)和动态流变学的变化,旨在揭示两者凝胶特性形成的差异。结果表明:在热诱导凝胶形成过程中,青鱼肌球蛋白变性展开程度高于鲢鱼肌球蛋白,暴露更多的疏水性氨基酸残基,从而形成的疏水性相互作用高于鲢鱼,使得青鱼肌球蛋白在热诱导凝胶形成过程中的dz约为鲢鱼肌球蛋白的2倍,G'高于鲢鱼。研究结果说明,青鱼肌球蛋白的热诱导凝胶形成能力高于鲢鱼,且二者肌球蛋白分子α-螺旋向β-折叠或β-转角转变有利于肌球蛋白的热凝胶作用。

     

    Abstract: The objective of this work was to investigate the difference of heat-induced gel properties between black carp(Mylopharyngodon piceus)and silver carp(Hypophthalmichthys molitrix). The secondary structure,surface hydrophobicity(S0-ANS),disulfide bonds,average particle size(dz)and dynamic rheology of myosin during heat-induced gel formation were also studied. The results showed that denaturation degree of black carp myosin was higher than that of silver carp during the heat-induced gel formation,indicating more hydrophobic amino acid residues were exposed to form a higher hydrophobic interaction in black carp myosin. Therefore,the dz of black carp myosin was about twice that of silver carp,and G' was higher than silver carp. The results showed that the myosin of black carp had a higher heat-induced gel forming ability than silver carp. The transformation of α-helix to β-fold or β-turn angle were conducive to the gelation of myosin.

     

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