Sequential extraction of gel-forming proteins, collagen and collagen hydrolysate from gutted silver carp (Hypophthalmichthys molitrix), a biorefinery approach
Sequential extraction of gel-forming proteins, collagen and collagen hydrolysate from gutted silver carp (Hypophthalmichthys molitrix), a biorefinery approach
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DOI：
10.1016/j.foodchem.2017.09.045
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发表时间：
2018-03-01
期刊：
影响因子：
8.8
通讯作者：
Undeland, Ingrid
中科院分区：
文献类型：
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作者：
Abdollahi, Mehdi;Rezaei, Masoud;Undeland, Ingrid
从含有pH-n(Shift-n)沉淀物残留物的骨骼和皮肤中回收胶原和胶原水解物(CH)。与酸或胃酶分离胶原蛋白(3.1-5.9%)相比，水解得率(15.1-15.4%)更高(p<；0.05)。经SDS-n(PAGE和FTIR)证实，分离的胶原蛋白为I型，并保持其三重n(螺旋)结构。胃蛋白酶和胃酶、胰酶的连续水解均可使所有大分子链的胶原蛋白发生水解性反应，但顺序水解液的水解度较高。当在凝胶前将CH加入到鲤鱼分离蛋白中时，凝胶行为取决于添加的CH的相对分子质量。更多的水解胶原蛋白从连续的水解中出现，提高了凝胶的保水能力，同时降低了其破碎力。因此，鱼的pH-n(变速)处理后的残渣可用于分离高质量的胶原/CH，并为多产品鱼的生物精炼提供了有希望的基础。
Collagen and collagen hydrolysate (CH) was recovered from the bone and skin containing sediment residue emerging during pH-n(shift-n(based protein isolation from silver carp. Hydrolysis resulted in higher yield (15.1-15.4%) compared to collagen isolation by acid or pepsin (3.1-5.9%) (p< 0.05). Isolated collagens were characterized as type I and maintained their triple-n(helical structure, confirmed by SDS-n(PAGE and FTIR. Pepsinhydrolysis and sequential hydrolysis by pepsin and trypsin hydrolyzed all heavy molecular weight chains of collagen but sequential hydrolysis yielded higher degree of hydrolysis. When CH was added to a silver carp protein isolate prior to gelation, the gel behavior was dependent on molecular weight of the added CH. More hydrolyzed collagen emerging from sequential hydrolysis improved water holding capacity of the gel while reducing its breaking force. Thus, residue from pH-n(shift processing of fish can be used for isolation of high quality collagen/CH and provides a promising basis for a multiple-product fish biorefinery.