Studies on the distribution of structural proteins in himodori kamaboko by immuno-electron microscopic technique and physical properties
Studies on the distribution of structural proteins in himodori kamaboko by immuno-electron microscopic technique and physical properties
批准号:
14560103
负责人:
TACHIBANA Katsuyasu
金额:
$2.11万
依托单位:
依托单位国家:
日本
项目类别:
Grant-in-Aid for Scientific Research (C)
财政年份:
2002
资助国家:
日本
项目状态:
已结题
起止时间:
2002 至 2004
中文摘要
以团头鱼和蜥蜴鱼为原料,制作了普通梭子鱼(两步加热:40℃120min→90℃30min)和海莫里梭子鱼(团头鱼:60℃20h→90℃30min,蜥蜴鱼:60℃120min→90℃30min)。用抗肌球蛋白、抗肌动蛋白和抗α-肌动蛋白血清,用免疫电子显微镜技术研究了Kamaboko的蛋白质分布。团头鱼的凝胶强度和断裂强度分别为1/2和1/4,而蜥蜴鱼则为1/3。两种鱼的正常kamaboko的超微结构均表现为弥散分布的小颗粒,而himodori kamaboko的超微结构显示出许多低密度部分和聚集的高密度颗粒。免疫电子显微镜观察发现,正常Kamaboko的弥漫部分布有较多的金粒子,而Himodori Kamaboko的聚集部分布的金粒子较少。当使用抗肌球蛋白血清时,这种现象尤其明显。在SDS-PAGE上的肌球蛋白条带及其免疫印迹结果显示,这两种鱼的肌球蛋白条带明显比正常的kamaboko颜色浅。
英文摘要
Normal kamaboko (two step heating:40℃120min→90℃30min) and himodori kamaboko (red sea bream:60℃20h→90℃30min, lizard fish:60℃120min→90℃30min) were made from red sea bream and lizard fish. Protein distribution in kamaboko was studied by immuno-electron microscopic technique using anti-myosin, anti-actin or anti-α-actinin serum. Physical properties (gel strength and breaking strength) were decrease in himodori kamaboko from red sea bream (1/2 in gel strength and 1/4 in breaking strength) and from lizard fish (1/3 in both of gel strength and breaking strength). Ultra structure of normal kamaboko from both fish showed homogeneous distribution of difluse smaller particles, however, himodori kamaboko showed many low density parts and aggregated high density particles. Using immuno-electron microscopic technique, many gold particles distributed on diflused part in normal kamaboko, on the other hand, few gold particles distributed on aggregated parts in himodori kamaboko. This phenomenon was specially observed when using anti-myosin serum. Myosin bands on SDS-PAGE and its immunoblotting of himodori kamaboko from both fish resulted on a remarkably lighter color than normal kamaboko.
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