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中国精品科技期刊2020
崔瑞颖, 焦学芹, 崔波, 祖铁红, 郑乾魏, 张志胜. 冻藏对海湾扇贝闭壳肌蛋白质变性及组织结构的影响[J]. 食品工业科技, 2013, (22): 298-301. DOI: 10.13386/j.issn1002-0306.2013.22.027
引用本文: 崔瑞颖, 焦学芹, 崔波, 祖铁红, 郑乾魏, 张志胜. 冻藏对海湾扇贝闭壳肌蛋白质变性及组织结构的影响[J]. 食品工业科技, 2013, (22): 298-301. DOI: 10.13386/j.issn1002-0306.2013.22.027
CUI Rui-ying, JIAO Xue-qin, CUI Bo, ZU Tie-hong, ZHENG Qian-wei, ZHANG Zhi-sheng. Effects of frozen storage on protein denaturation and structure of Argopecten irradiams muscle[J]. Science and Technology of Food Industry, 2013, (22): 298-301. DOI: 10.13386/j.issn1002-0306.2013.22.027
Citation: CUI Rui-ying, JIAO Xue-qin, CUI Bo, ZU Tie-hong, ZHENG Qian-wei, ZHANG Zhi-sheng. Effects of frozen storage on protein denaturation and structure of Argopecten irradiams muscle[J]. Science and Technology of Food Industry, 2013, (22): 298-301. DOI: 10.13386/j.issn1002-0306.2013.22.027

冻藏对海湾扇贝闭壳肌蛋白质变性及组织结构的影响

Effects of frozen storage on protein denaturation and structure of Argopecten irradiams muscle

  • 摘要: 以海湾扇贝闭壳肌盐溶性蛋白含量、肌原纤维蛋白Ca2+-ATPase活性及组织的显微镜观察为指标,研究了冻藏条件对海湾扇贝闭壳肌蛋白质变性及组织结构的影响。结果表明,冷藏过程中蛋白质发生变性,盐溶性蛋白及肌原纤维蛋白Ca2+-ATPase活性显著下降(p<0.05);贮藏1575d时间内,(-35±1)℃下的闭壳肌盐溶性蛋白含量高于(-25±1)℃,且有显著差异(p<0.05);贮藏过程中,(-35±1)℃下闭壳肌的肌原纤维蛋白Ca2+-ATPase活性高于(-25±1)℃,除贮藏0d、45d差异不显著外,其余相同贮藏时间内不同冻藏温度对肌原纤维蛋白Ca2+-ATPase活性影响差异显著(p<0.05)。(-35±1)℃冻藏条件下海湾扇贝闭壳肌肌肉纤维相对(-25±1)℃冻藏组织结构更加完整。因此,选择(-35±1)℃冻藏海湾扇贝闭壳肌对蛋白质及组织结构的变化影响较好。 

     

    Abstract: Changes of salt solubility protein, the Ca2+-ATPase activity in myofibrillar protein and the structure of Argopecten irradiams muscle were studied during storage at two different temperatures ( (-25±1) ℃, (-35±1) ℃) .Results showed that during frozen storage, salt solubility protein and the Ca2 +-ATPase activity in myofibrillar protein was reduction signifienatly (p<0.05) . Argopecten irradiams muscle storage at two different temperatures ( (-25±1) ℃, (-35±1) ℃) ) , salt solubility protein changed signifienatly during storage time at 1575d (p<0.05) .In the process of storage, the Ca2 +-ATPase activity in myofibrillar protein changed signifienatly at different frozen storage temperatures except storage time at 0d and 45d (p<0.05) . Structure of Argopecten irradiams muscle frozen storage temperatures at (- 35 ± 1) ℃ was more complete than the storage temperatures at (-25±1) ℃. So (-35±1) ℃ was better on protein denaturation and structure of Argopecten irradiams muscle.

     

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