期刊
RSC ADVANCES
卷 11, 期 31, 页码 19158-19168出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/d1ra00657f
关键词
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资金
- Shaanxi Provincial Department of Science and Technology [2019NY-133, 2021NY-132]
- Key Laboratory of Se-enriched Products Development and Quality Control (Ministry of Agriculture)
- National and Local Joint Engineering Laboratory for Selenium-enriched Food Development [Se-2019B03]
- Undergraduate Innovation and Entrepreneurship Training Program of Shaanxi Xueqian Normal University [2020DC090]
The modification of defatted walnut meal protein glutelin-1 by pepsin enzymatic hydrolysis improved its functional properties and antioxidant activities, demonstrating better physicochemical properties and stronger antioxidant activities compared to unmodified protein.
Glutelin-1 of defatted walnut meal protein (DWPG-1) was modified by pepsin enzymatic hydrolysis to improve its functional properties and antioxidant activities. The amino acid composition, structural characteristics, physicochemical and functional properties as well as antioxidant activities of the hydrolysate were compared with those of unmodified DWPG-1. The analysis of X-ray diffraction patterns, surface microstructure and particle size distribution indicated that enzymatic hydrolysis changed the structures of DWPG-1. Compared with the natural unhydrolyzed protein, the hydrolysate showed better physicochemical properties, such as surface hydrophobicity, solubility, emulsifying properties, foaming properties and water absorption capacity. In addition, the hydrolysate also exhibited significantly stronger antioxidant activities than DWPG-1. In conclusion, the results of this study prove that pepsin-mediated hydrolysis of walnut glutelin-1 can effectively modify the structure, function and antioxidant activity of DWPG-1, and could be used as an effective technology to produce bioactive multifunctional hydrolysates.
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