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超声波辅助酶法提取牛皮胶原蛋白及其结构表征
引用本文:赵改名,王壮壮,祝超智,余小领,张秋会,祁兴山.超声波辅助酶法提取牛皮胶原蛋白及其结构表征[J].食品工业科技,2023,44(9):190-199.
作者姓名:赵改名  王壮壮  祝超智  余小领  张秋会  祁兴山
作者单位:1.河南农业大学食品科学技术学院,河南郑州 4500022.恒都综合试验站,河南驻马店 463000
基金项目:财政部和农业农村部:国家现代农业(肉牛牦牛)产业技术体系建设专项(CARS-37)
摘    要:以牛皮为原料,优化超声波辅助酶提取牛皮中胶原蛋白的工艺。在单因素实验的基础上设计响应面试验,以牛皮胶原蛋白提取率为响应值,优化得到胶原蛋白的最佳提取工艺,并对其进行结构表征。结果表明:牛皮中胶原蛋白的最佳提取工艺条件为超声波功率161 W、超声波处理时间64 min、胃蛋白酶添加量109 U/g、料液比1:16 g/mL,在此条件下胶原蛋白的提取率为63.77%。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(SDS-PAGE)、紫外光谱(UV)和傅立叶红外光谱(FTIR)分析表明,超声波辅助酶提取的胶原蛋白符合Ⅰ型胶原蛋白的特征,保持了其完整的三螺旋结构,氨基酸组成和扫描电镜(SEM)分析得到超声波辅助酶提取的胶原蛋白三螺旋稳定程度略微下降。本研究为牛皮中胶原蛋白的提取优化了一种有效的工艺,且很大程度上缩短了胶原蛋白的提取时间,并且具有较高的应用价值。

关 键 词:牛皮胶原蛋白  超声波  提取率  工艺优化  结构表征
收稿时间:2022-07-19

Ultrasound-Assisted Enzymatic Extraction and Structural Characterization of Cowhide Collagen
ZHAO Gaiming,WANG Zhuangzhuang,ZHU Chaozhi,YU Xiaoling,ZHANG Qiuhui,QI Xingshan.Ultrasound-Assisted Enzymatic Extraction and Structural Characterization of Cowhide Collagen[J].Science and Technology of Food Industry,2023,44(9):190-199.
Authors:ZHAO Gaiming  WANG Zhuangzhuang  ZHU Chaozhi  YU Xiaoling  ZHANG Qiuhui  QI Xingshan
Affiliation:1.College of Food Science and Technology, Henan Agricultural University, Zhengzhou 450002, China2.Hengdu Comprehensive Experimental Station, Zhumadian 463000, China
Abstract:Using cowhide as raw material, the process of ultrasonic-assisted enzyme extraction of collagen from cowhide was optimized. Based on the single factor experiment, a response surface test was designed, and the extraction rate of cowhide collagen was used as the response value to optimize the optimal extraction process of collagen, and its structure was characterized. The results showed that the optimal extraction conditions of collagen from cowhide were ultrasonic power 161 W, ultrasonic treatment time 64 min, pepsin addition 109 U/g, and solid-liquid ratio 1:16 g/mL. Under these conditions, the extraction rate of collagen was 63.77%. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), ultraviolet spectroscopy (UV) and Fourier transform infrared spectroscopy (FTIR) analysis showed that the collagen extracted by ultrasound-assisted enzyme was in line with the characteristics of type I collagen, maintaining its complete triple helix structure, amino acid composition and scanning electron microscope (SEM) analysis showed that the collagen triple helix extracted by ultrasonic assisted enzyme was relatively stable. In this study, an effective process is optimized for the extraction of collagen from cowhide, besides, the extraction time of collagen is greatly shortened and it has high utilization value.
Keywords:
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