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作 者:宫萱 包建强[1] 黄可承 陈彦婕 唐嘉诚 Gong Xuan;Bao Jianqiang;Huang Kecheng;Chen Yanjie;Tang Jiacheng(College of Food Science,Shanghai Ocean University,Shanghai 201306)
出 处:《中国食品学报》2024年第3期268-275,共8页Journal of Chinese Institute Of Food Science and Technology
基 金:水产动物遗传育种中心上海市协同创新中心项目(ZF1206);上海市科委工程中心建设项目(11DZ2280300)。
摘 要:大鲵为一种珍贵的两栖动物,营养丰富。为了充分且有效利用其加工副产物,分离并表征了来自大鲵骨的酸溶性胶原蛋白(ASC)和胃蛋白酶溶解性胶原蛋白(PSC)。大鲵骨ASC和PSC的产率分别为10.71%和13.11%。通过傅里叶红外光谱揭示胶原蛋白稳定的三螺旋结构。SDS-PAGE电泳图显示两个样品均为I型胶原蛋白,同时具有高水平的亚氨基酸(179~187/1000个残基)。样品在pH 6时溶解度最高。热变性温度(45.78~46.51℃)显著高于海洋和淡水鱼物种。在SEM下,胶原蛋白显示出致密的片状和不规则的孔洞状。这些结果表明大鲵骨胶原蛋白特性与哺乳动物胶原蛋白相似,具有成为其替代品的潜力,为其后续的研究和开发利用提供了基础数据。The giant salamander,as a precious amphibian,is rich in nutritional value.To fully and efficiently utilize its processing by-products,acid-soluble collagen(ASC)and pepsin-soluble collagen(PSC)from giant salamander bone were isolated and characterized.The yields of salamander bone ASC and PSC were 10.71%and 13.11%,respectively.The stable triple helical structure of collagen was revealed by Fourier transform infrared spectroscopy.SDS-PAGE electropherograms showed that both samples were type I collagen with high levels of imino acids(179-187/1000 residues).Their solubility was highest at pH 6.The thermal denaturation temperature(45.78-46.51℃)was significantly higher than that of marine and freshwater fish species.Under SEM,the collagen showed dense flakes and irregular holes.These results show that the characteristics of giant salamander bone collagen are similar to mammalian collagen,and it has the potential to become its substitute,which provides a basis for its subsequent research and development and utilization.
分 类 号:TS254.9[轻工技术与工程—水产品加工及贮藏工程]
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