Acid-soluble collagen (ASC) and pepsin-solubilized collagen (PSC) were prepared from the waste freshwater carp fish scales. The results of SDS-PAGE showed that purified collagens were composed of at least two differen...Acid-soluble collagen (ASC) and pepsin-solubilized collagen (PSC) were prepared from the waste freshwater carp fish scales. The results of SDS-PAGE showed that purified collagens were composed of at least two different chains which were in accordance with the type I collagen with α chain composition of (α1)2α2. Compared with the carp fish ordinary muscle type I collagen , porcine dermis type I collagen and other seawater fish collagens, freshwater carp fish scales collagen contained relative high half-cystine (Cys-s), but lower denaturation temperature(Td) than the porcine dermis type I collagen. These collagens had evident absorption at 230 nm by UV-Vis spectra. The spectrum X-ray diffraction showed that the collagen remained single-helix and tri-helix configuration with the minimum values of the repeat spacings (d) of about 4.48 ? and 11.87 ?. Therefore, to make more effective use of limited-resources, carp fish scales can be a potential resource for the extraction of type I collagen or gelatin.展开更多
本实验以鲢鱼骨为原料制成纳米鱼骨(nano-scaled fish bone,NFB)、微米鱼骨(micro-scaled fish bone,MFB),并以CaCl2为对照,将其加入至鲢鱼肌球蛋白中,通过静态流变学、动态流变学、表面疏水性分析以及活性巯基浓度和溶解度的测定,比较...本实验以鲢鱼骨为原料制成纳米鱼骨(nano-scaled fish bone,NFB)、微米鱼骨(micro-scaled fish bone,MFB),并以CaCl2为对照,将其加入至鲢鱼肌球蛋白中,通过静态流变学、动态流变学、表面疏水性分析以及活性巯基浓度和溶解度的测定,比较不同钙源对肌球蛋白凝胶性能的影响。结果表明:各组肌球蛋白样品均具有剪切稀化现象,NFB和CaCl2的添加均会增加肌球蛋白的表观黏度,MFB则相反,这与NFB和CaCl2释放出的钙离子促进了蛋白质分子间的相互作用密切相关,而MFB由于颗粒较大,干扰了蛋白质分子间相互作用。加热过程中,NFB和CaCl2的添加进一步促进肌球蛋白通过形成二硫键和疏水相互作用,使肌球蛋白黏弹性升高。NFB对肌球蛋白胶凝特性的提升作用与CaCl2相近,明显高于MFB组,这为今后将NFB应用于鱼糜制品中提供了一定的数据支撑。展开更多
文摘Acid-soluble collagen (ASC) and pepsin-solubilized collagen (PSC) were prepared from the waste freshwater carp fish scales. The results of SDS-PAGE showed that purified collagens were composed of at least two different chains which were in accordance with the type I collagen with α chain composition of (α1)2α2. Compared with the carp fish ordinary muscle type I collagen , porcine dermis type I collagen and other seawater fish collagens, freshwater carp fish scales collagen contained relative high half-cystine (Cys-s), but lower denaturation temperature(Td) than the porcine dermis type I collagen. These collagens had evident absorption at 230 nm by UV-Vis spectra. The spectrum X-ray diffraction showed that the collagen remained single-helix and tri-helix configuration with the minimum values of the repeat spacings (d) of about 4.48 ? and 11.87 ?. Therefore, to make more effective use of limited-resources, carp fish scales can be a potential resource for the extraction of type I collagen or gelatin.
文摘本实验以鲢鱼骨为原料制成纳米鱼骨(nano-scaled fish bone,NFB)、微米鱼骨(micro-scaled fish bone,MFB),并以CaCl2为对照,将其加入至鲢鱼肌球蛋白中,通过静态流变学、动态流变学、表面疏水性分析以及活性巯基浓度和溶解度的测定,比较不同钙源对肌球蛋白凝胶性能的影响。结果表明:各组肌球蛋白样品均具有剪切稀化现象,NFB和CaCl2的添加均会增加肌球蛋白的表观黏度,MFB则相反,这与NFB和CaCl2释放出的钙离子促进了蛋白质分子间的相互作用密切相关,而MFB由于颗粒较大,干扰了蛋白质分子间相互作用。加热过程中,NFB和CaCl2的添加进一步促进肌球蛋白通过形成二硫键和疏水相互作用,使肌球蛋白黏弹性升高。NFB对肌球蛋白胶凝特性的提升作用与CaCl2相近,明显高于MFB组,这为今后将NFB应用于鱼糜制品中提供了一定的数据支撑。
