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中国精品科技期刊2020
任戈一,马雪莲,潘丽,等. 不同提取工艺下牛骨胶原蛋白的结构特性[J]. 食品工业科技,2022,43(14):27−33. doi: 10.13386/j.issn1002-0306.2021090282.
引用本文: 任戈一,马雪莲,潘丽,等. 不同提取工艺下牛骨胶原蛋白的结构特性[J]. 食品工业科技,2022,43(14):27−33. doi: 10.13386/j.issn1002-0306.2021090282.
REN Geyi, MA Xuelian, PAN Li, et al. Structural Characteristics of Bovine Bone Collagen under Different Extraction Processes[J]. Science and Technology of Food Industry, 2022, 43(14): 27−33. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2021090282.
Citation: REN Geyi, MA Xuelian, PAN Li, et al. Structural Characteristics of Bovine Bone Collagen under Different Extraction Processes[J]. Science and Technology of Food Industry, 2022, 43(14): 27−33. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2021090282.

不同提取工艺下牛骨胶原蛋白的结构特性

Structural Characteristics of Bovine Bone Collagen under Different Extraction Processes

  • 摘要: 为提高牛骨资源的利用率,以新鲜牛骨为原料,分别采用乙酸、柠檬酸、乙酸和胃蛋白酶、柠檬酸和胃蛋白酶提取得到四种牛骨胶原蛋白(ASC1、ASC2、PSC1和PSC2)并通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(SDS-PAGE),傅里叶红外光谱(FTIR),扫描电镜(SEM),表面疏水性等指标对其理化性质和结构特征进行研究。结果表明:PSC1的得率最高,可达3.23%,四种提取方法得到的胶原蛋白均于230 nm附近出现最大紫外吸收峰;SDS-PAGE和红外光谱分析表明牛骨胶原蛋白主要由α1α2β三种亚基成分组成,属于 I型胶原蛋白,且胶原蛋白的空间结构保留完整;扫描电镜直观表明了四种胶原蛋白的纤维网络结构均保留较完整,其中酸法提取的胶原蛋白(ASC1和ASC2)网络结构分布较为均匀;酶法制得的胶原蛋白(PSC1和PSC2)纤维化较为明显,四种胶原蛋白理化特性无显著差异,但微观结构存在一定差异。本研究为提高畜禽副产物高值化应用发展及深加工技术提供了一定的理论基础。

     

    Abstract: In order to improve the utilization rate of bovine bone resources, fresh bovine bone was used as raw material, four kinds of bovine bone collagen (ASC1, ASC2, PSC1 and PSC2) were extracted by acetic acid, citric acid, acetic acid and pepsin, citric acid and pepsin, the physicochemical properties and structural characteristics were studied by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), fourier transform infrared spectroscopy (FTIR), scanning electron microscopy (SEM), surface hydrophobicity and other indicators. The results showed that PSC1 had the highest yield, which was 3.23%, the maximum ultraviolet absorption peak of the collagen extracted by four kinds of extraction methods were found around 230 nm. SDS-PAGE and infrared spectroscopy analysis showed that four kinds of collagen were composed of α1, α2 and β subunits, which belonged to type I collagen and the space structure of bovine collagen was preserved intact. Scanning electron microscopy showed that the fiber network structure of the four kinds of collagen (acid method and enzyme method) were relatively intact, among the network structure of the collagen extracted by acid method (ASC1 and ASC2) was evenly distributed. The collagen extracted by enzymatic method (PSC1 and PSC2) had obvious fibrosis. There was no significant difference in the physicochemical properties of the four kinds of collagen, but there were some differences in the microstructure. This study would provide a theoretical basis for improving the development of high value application and deep processing technology of livestock and poultry by-products.

     

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