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牛屠宰行业副产品的增值利用:高静水压对牛皮明胶功能特性和结构特征的影响

Valorization of Cattle Slaughtering Industry By-Products: Modification of the Functional Properties and Structural Characteristics of Cowhide Gelatin Induced by High Hydrostatic Pressure.

作者信息

Gao Yanlei, Wang Liyuan, Qiu Yi, Fan Xiaona, Zhang Li, Yu Qunli

机构信息

College of Food Science and Engineering, Gansu Agriculture University, Lanzhou 730070, China.

出版信息

Gels. 2022 Apr 14;8(4):243. doi: 10.3390/gels8040243.

DOI:10.3390/gels8040243
PMID:35448144
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9029605/
Abstract

This study investigates the effects of different pressures (200, 250, 300, 350, and 400 MPa) and durations (5, 10, 15, 20, and 25 min) on the functional properties, secondary structure, and intermolecular forces of cowhide gelatin. Our results show that high hydrostatic pressure significantly affected the two, three, and four-level structures of gelatin and caused the contents of the α-helix and β-turn to decrease by 68.86% and 78.58%, respectively (p < 0.05). In particular, the gelatin at 300 MPa for 15 min had the highest gel strength, emulsification, solubility, and foaming of all the treatment conditions under study. The analysis of the surface hydrophobicity, sulfhydryl content, zeta potential, and Raman spectroscopy shows that at a pressure of 300 MPa (15 min), the hydrogen bonds and hydrophobic interactions between collagen molecules are strongly destroyed, leading to changes in the tertiary and quaternary conformation of the protein and unfolding, with the electrostatic repulsion between protein particles making the decentralized state stable. In conclusion, moderate pressure and time can significantly improve the functional and structural properties of collagen, which provides theoretical support and guidance for realizing the high-value utilization of cowhide.

摘要

本研究考察了不同压力(200、250、300、350和400兆帕)和持续时间(5、10、15、20和25分钟)对牛皮明胶功能特性、二级结构和分子间作用力的影响。我们的结果表明,高静水压显著影响了明胶的二、三、四级结构,导致α-螺旋和β-转角含量分别下降了68.86%和78.58%(p<0.05)。特别是,在所有研究的处理条件下,300兆帕处理15分钟的明胶具有最高的凝胶强度、乳化性、溶解性和发泡性。表面疏水性、巯基含量、zeta电位和拉曼光谱分析表明,在300兆帕(15分钟)的压力下,胶原分子之间的氢键和疏水相互作用被强烈破坏,导致蛋白质三级和四级构象发生变化并展开,蛋白质颗粒之间的静电排斥使分散状态稳定。总之,适度的压力和时间可以显著改善胶原的功能和结构特性,这为实现牛皮的高值利用提供了理论支持和指导。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/026a/9029605/3d8e38f653fd/gels-08-00243-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/026a/9029605/31b85e82e266/gels-08-00243-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/026a/9029605/ca88159f4328/gels-08-00243-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/026a/9029605/504320306f31/gels-08-00243-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/026a/9029605/3d8e38f653fd/gels-08-00243-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/026a/9029605/31b85e82e266/gels-08-00243-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/026a/9029605/ca88159f4328/gels-08-00243-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/026a/9029605/504320306f31/gels-08-00243-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/026a/9029605/3d8e38f653fd/gels-08-00243-g004.jpg

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