食品科学 ›› 2018, Vol. 39 ›› Issue (12): 101-106.doi: 10.7506/spkx1002-6630-201812016

• 食品化学 • 上一篇    下一篇

酸法和酶法提取牦牛骨胶原蛋白的特性分析

王晓军1,2,吴婷1,2,贾伟1,2,张春晖2,韩玲1,*,余群力1   

  1. (1.甘肃农业大学食品科学与工程学院,甘肃?兰州 730070;2.中国农业科学院农产品加工研究所,北京 100193)
  • 出版日期:2018-06-25 发布日期:2018-06-15
  • 基金资助:
    现代农业产业技术体系建设专项(CARS-38);农业部“948”项目(2016-X31)

Comparative Analysis of Collagen Extracted from Yak Bones Using Acidic and Enzymatic Treatment

WANG Xiaojun1,2, WU Ting1,2, JIA Wei1,2, ZHANG Chunhui2, HAN Ling1,*, YU Qunli1   

  1. (1. College of Food Science and Engineering, Gansu Agricultural University, Lanzhou 730070, China; 2. Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing 100193, China)
  • Online:2018-06-25 Published:2018-06-15

摘要: 以牦牛骨为原料,分别采用酸法和酶法提取胶原蛋白并进行理化性质分析。通过氨基酸组成、紫外光谱、傅里叶变换红外光谱、热收缩温度、十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(sodium dodecyl sulfate-polyacrylamide gelelectrophoresis,SDS-PAGE)和扫描电子显微镜图像分析对胶原蛋白进行比较。结果表明:2?种方法的提取物都为典型的胶原蛋白,在230?nm波长左右出现最大紫外吸收峰;酸溶胶原蛋白(acid-soluble collagen,ASC)和酶溶胶原蛋白(pepsin-soluble collagen,PSC)的热收缩温度分别为40.12?℃和40.94?℃,变性焓值分别为0.25?J/g和0.22?J/g;红外光谱及SDS-PAGE分析表明,ASC和PSC主要由α、β、γ三种亚基组分组成,属于I型胶原蛋白,且三股螺旋结构完整;扫描电子显微镜结果表明,2?种方法提取的胶原蛋白都保留了较为完整的纤维网状结构,但酸法提取的胶原蛋白结构分布相对均匀。综合来看,2?种方法所提胶原蛋白在理化特性上并无太大差别,但酶法提取的胶原蛋白得率较高,酸法提取成本较低。

关键词: 牦牛骨, 胶原蛋白, 酸法, 酶法

Abstract: Acidic and enzymatic extraction methods were separately used to extract collagen from yak bone and the physicochemical properties of the obtained collagens were compared. Their amino acid compositions were analyzed and their structures were determined by using UV spectroscopy, Fourier transform infrared spectroscopy (FTIR), heat shrinkage temperature, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and scanning electron microscopy (SEM). The extracts were characterized as collagens, showing maximum UV absorption peak at 230 nm. The heat shrinkage temperatures of acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) were 40.12 and 40.94 ℃, respectively, and their denaturation enthalpies were 0.25 and 0.22 J/g, respectively. FTIR and SDS-PAGE analyses demonstrated that ASC and PSC were mainly composed of α, β and γ subunit components, which both belonged to type I collagen with a complete three-strand helical structure. SEM revealed that ASC and PSC retained a relatively complete fibrous network structure, but the structure of ASC was more evenly distributed. There was no significant difference in the physiochemical properties of the two collagens, while the enzymatic extraction method gave a higher yield of collagen but was more expensive than acidic extraction.

Key words: yak bone, collagen, acidic extraction method, enzymatic extraction method

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