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从深海红鱼(Sebastes mentella)皮肤中分离和鉴定胶原蛋白。

Isolation and characterization of collagen from the skin of deep-sea redfish (Sebastes mentella).

作者信息

Wang L, An X, Xin Z, Zhao L, Hu Q

机构信息

Key Laboratory of Food Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural Univ., Nanjing 210095, P.R. China.

出版信息

J Food Sci. 2007 Oct;72(8):E450-5. doi: 10.1111/j.1750-3841.2007.00478.x.

DOI:10.1111/j.1750-3841.2007.00478.x
PMID:17995604
Abstract

To make more effective use of underutilized resources, acid-solubilized collagen (ASC) and pepsin-solubilized collagen (PSC) were isolated from the skin of deep-sea redfish (Sebastes mentella) and characterized for their potential in commercial applications. The yield of ASC (47.5%) was lower compared to PSC (92.2%), but the purity of ASC was significantly higher. The intrinsic viscosity of ASC (15.9 dL/g) was greater than PSC (14.6 dL/g), indicating a higher average molecular weight of ASC on account of the high proportion of polymers of collagen. The denaturation temperatures of ASC and PSC were 16.1 and 15.7 degrees C, respectively, suggesting the triple helical structure of PSC was still predominant. The amino acid profiles of ASC and PSC were similar with lower imino acid content than most other species, which might be the reason for the lower denaturation temperature. SDS-PAGE and FTIR showed that both ASC and PSC were type I mainly with slight structure differences. ASC held its triple helical structure well, and possessed a higher extent of intermolecular cross-link. While the structure of PSC was changed slightly due to the loss of N- and C-terminus domains, the triple helical structure was still predominant as a result of the formation of more and/or stronger hydrogen bond.

摘要

为了更有效地利用未充分利用的资源,从深海红鱼(Sebastes mentella)的皮肤中分离出酸溶性胶原蛋白(ASC)和胃蛋白酶溶性胶原蛋白(PSC),并对它们在商业应用中的潜力进行了表征。与PSC(92.2%)相比,ASC的产率(47.5%)较低,但ASC的纯度显著更高。ASC的特性粘度(15.9 dL/g)大于PSC(14.6 dL/g),这表明由于胶原蛋白聚合物比例较高,ASC的平均分子量更高。ASC和PSC的变性温度分别为16.1和15.7摄氏度,这表明PSC的三螺旋结构仍然占主导地位。ASC和PSC的氨基酸谱相似,亚氨基酸含量低于大多数其他物种,这可能是变性温度较低的原因。SDS-PAGE和FTIR表明,ASC和PSC主要都是I型,只是结构略有差异。ASC能很好地保持其三螺旋结构,并具有更高程度的分子间交联。虽然PSC的结构由于N端和C端结构域的丢失而略有变化,但由于形成了更多和/或更强的氢键,三螺旋结构仍然占主导地位。

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