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从贻贝足丝中提取胶原蛋白:一种具有工业应用价值物理化学性质的新型海洋胶原蛋白来源。

Collagen extraction from mussel byssus: a new marine collagen source with physicochemical properties of industrial interest.

作者信息

Rodríguez F, Morán L, González G, Troncoso E, Zúñiga R N

机构信息

Department of Biotechnology, Universidad Tecnológica Metropolitana, Las Palmeras 3360, Ñuñoa, Santiago Chile.

Department of Chemical and Biochemical Engineering, Instituto Tecnológico de Zacatepec, Calzada Tecnológico 27, Zacatepec, Morelos Mexico.

出版信息

J Food Sci Technol. 2017 Apr;54(5):1228-1238. doi: 10.1007/s13197-017-2566-z. Epub 2017 Mar 6.

Abstract

Mussel byssus is a by-product of mussel production and is a potential source of collagen. The goal of this study was to extract collagen from the byssus of Chilean mussel using an enzymatic method and characterize it. A pepsin-aided extraction method was employed where first an enzymatic hydrolysis at two pepsin/substrate ratios (1:50 or 4:50) and times (4 or 24 h) was done. Extraction was conducted at 80 °C for 24 h, in a 0.5 N acetic acid solution. All samples were analyzed for collagen content, amino acid profile, turbidity, viscosity, solubility, denaturation temperature and surface tension. Hydrolysis time had significant effect on collagen content, hydroxyproline content and extraction yield. Hydrolysis with a pepsin/byssus ratio of 4:50 for 24 h gave the better extraction performance with values of 69 mg/g protein, 1.8 mg/g protein and 30%, for collagen content, hydroxyproline content and extraction yield, respectively. No differences were found for the viscosity and surface tension of collagen dispersions, suggesting that the enzymatic hydrolysis did not affect the integrity of the collagen molecule. Denaturation temperature of freeze-dried byssus collagen presented a high value (83-91 °C), making this kind of collagen a very interesting material for encapsulation of bioactive molecules and for biomedical applications.

摘要

贻贝足丝是贻贝生产的副产品,是胶原蛋白的潜在来源。本研究的目的是采用酶法从智利贻贝的足丝中提取胶原蛋白并对其进行表征。采用胃蛋白酶辅助提取方法,首先在两种胃蛋白酶/底物比例(1:50或4:50)和时间(4或24小时)下进行酶水解。在80℃下于0.5N乙酸溶液中进行提取24小时。对所有样品进行胶原蛋白含量、氨基酸谱、浊度、粘度、溶解度、变性温度和表面张力分析。水解时间对胶原蛋白含量、羟脯氨酸含量和提取率有显著影响。胃蛋白酶/足丝比例为4:50水解24小时时提取性能更佳,胶原蛋白含量、羟脯氨酸含量和提取率分别为69mg/g蛋白质、1.8mg/g蛋白质和30%。胶原蛋白分散体的粘度和表面张力未发现差异,表明酶水解未影响胶原蛋白分子的完整性。冻干的足丝胶原蛋白变性温度较高(83-91℃),使得这种胶原蛋白成为用于生物活性分子包封和生物医学应用的非常有吸引力的材料。

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