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作 者:崔瑞颖[1] 焦学芹[1] 祖铁红[1] 张志胜[1] 崔波[1] 张欣彩
出 处:《食品科技》2014年第2期134-138,共5页Food Science and Technology
基 金:国家海洋局海洋公益性行业科研专项(201205031)
摘 要:以海湾扇贝闭壳肌TBA值、肌原纤维蛋白Ca2+-ATPase活性及组织的显微镜观察为指标,研究了不同冷冻方式[(-25±1)℃冰箱冷冻、(-35±1)℃冰柜冷冻、(-80±1)℃超低温冷冻和液氮冷冻]对海湾扇贝闭壳肌大分子物质及组织结构的影响。研究结果表明:相同冷冻方式条件下,冻藏时间对其TBA值及肌原纤维蛋白Ca2+-ATPase活性影响显著(p<0.05);相同冻藏时间条件下,不同的冷冻方式对海湾扇贝闭壳肌的TBA值影响差异均显著(p<0.05),液氮处理对肌原纤维蛋白Ca2+-ATPase活性影响与其他处理间差异显著(p<0.05),其他3种处理间差异不显著。由光学显微镜下图片可知,液氮处理对海湾扇贝闭壳肌肌肉纤维的影响最小,与新鲜闭壳肌的结构最相近,(-25±1)℃冰箱冷冻对闭壳肌肌肉纤维结构破坏最大。因此,选择(-35±1)℃冰柜冷冻海湾扇贝闭壳肌对大分子物质及组织结构的变化影响较好。Taking TBA, the Ca2+-ATPase activity in myofibrillar protein and the structure of Argopecten irradiams muscle as the indexes, the effects of 4 different freezing processes, such as(-25±1) ℃ refrigerator freezing,(-35±1) ℃ refrigerator freezing,(-80±1) ℃ ultra-low temperature freezing and liquid nitrogen freezing, on biomacromolecules and structure of Argopecten irradiams muscle were studied. Results showed that: At the same freezing process, TBA and the Ca2+-ATPase activity in myofibrillar protein change signifienatly at different frozen storage time(p0.05); at the same frozen storage time, TBA change signifienatly at different freezing processes(p0.05), the Ca2+-ATPase activity in myofibrillar protein change signifienatly between liquid nitrogen freezing and other freezing processes(p0.05). By optical microscope images, Argopecten irradiams muscle structure by liquid nitrogen freezing similar to the fresh muscle structure. The change of muscle fiber structure is the largest by(-25±1) ℃ refrigerator freezing of Argopecten irradiams muscle. So,(-35±1) ℃ refrigerator freezing was better on on biomacromolecules andstructure of Argopecten irradiams muscle.
分 类 号:TS254.4[轻工技术与工程—水产品加工及贮藏工程]
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