Effect of protein hydrolysis on the emulsifying properties of collagen and its hydrolysates extracted from leather by-products

IF 2.4 4区生物学 Q3 BIOTECHNOLOGY & APPLIED MICROBIOLOGY

Journal of chemical technology and biotechnology Pub Date : 2025-07-04 DOI:10.1002/jctb.70001

Megan Phee, Warren Bowden, Stephen Euston, Stephen Hems, Nik Willoughby, Kelly Stewart

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引用次数: 0

Abstract

Background

Proteins are widely used as emulsifiers due to their amphiphilic nature. Collagen has been of particular interest due to both its distinctive triple helical structure and unique amino acid arrangement, which gives it strength and stability within the water (hydrophilic) and oil (hydrophobic) domains of the emulsion. Hydrolysing collagen reveals varying amino acid side residues and alters its interaction with water/oil interfaces. This study aimed to explore how the degree of hydrolysation influences the protein's ability to act as an emulsifier, focusing on hydrolysed collagen derived from leather industry by-products.

Results

The results revealed that the optimal degree of protein hydrolysis was dependent on both the environment and the length of stability required of the emulsion. In this work, the least hydrolysed collagen sample had the most versatile properties in both cool and hot conditions, however due to the larger molecular size of the protein it also had a lower stability when measured over an extended time. A more hydrolysed form of collagen formed a stable emulsion at cool temperatures, however the breakdown of the emulsion observed at 40 °C indicated the need for further protein purification. Further hydrolysing the collagen caused a breakdown of the liquid emulsions at 4 °C due to gel formation, however this form of collagen performed best when held at elevated temperatures.

Conclusion

The results of this study concluded that the degree of hydrolysation of collagen could be manipulated to produce a tailored emulsifying agent dependent on the desired commercial end-use. © 2025 Scottish Leather Group and The Author(s). Journal of Chemical Technology and Biotechnology published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry (SCI).

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蛋白质水解对皮革副产物中胶原蛋白及其水解产物乳化性能的影响

蛋白质由于其两亲性而被广泛用作乳化剂。胶原蛋白由于其独特的三螺旋结构和独特的氨基酸排列，使其在乳液的水（亲水）和油（疏水）域内具有强度和稳定性而引起了特别的兴趣。水解胶原蛋白显示不同的氨基酸侧残基，并改变其与水/油界面的相互作用。本研究旨在探讨水解程度如何影响蛋白质作为乳化剂的能力，重点研究来自皮革工业副产品的水解胶原蛋白。结果乳状液的最佳水解程度取决于环境和乳状液所需的稳定时间。在这项工作中，最少水解的胶原蛋白样品在冷热条件下都具有最通用的特性，然而，由于蛋白质的分子大小较大，在长时间测量时稳定性也较低。一种水解程度更高的胶原蛋白在低温下形成稳定的乳液，然而，在40°C下观察到的乳液的分解表明需要进一步的蛋白质纯化。进一步水解胶原蛋白导致液体乳剂在4°C时由于凝胶形成而破裂，然而这种形式的胶原蛋白在高温下表现最好。结论本研究的结果表明，胶原蛋白的水解程度可以根据所需的商业最终用途进行调整，以生产定制的乳化剂。©2025苏格兰皮革集团和作者。由John Wiley &； Sons Ltd代表美国化学工业学会（SCI）出版的化学技术与生物技术杂志。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Journal of chemical technology and biotechnology 工程技术-工程：化工

CiteScore

7.00

自引率

5.90%

发文量

268

审稿时长

1.7 months

期刊介绍： Journal of Chemical Technology and Biotechnology(JCTB) is an international, inter-disciplinary peer-reviewed journal concerned with the application of scientific discoveries and advancements in chemical and biological technology that aim towards economically and environmentally sustainable industrial processes.