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Changes of structure and function of enzymatic hydrolysates of walnut protein isolate |
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DOI: |
KeyWord:walnut protein isolate protease structure functionality |
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Author Name | Affiliation | CHENG Zan1, ZHAO Xiaoyan1, ZHANG Xiaowei1, WANG Meng1, LIU Hongkai1, HU Haifang2 | 1.Food Science and Nutrition Department, University of Jinan, Jinan 250022, China 2.Xinjiang Academy of Forestry Sciences, Urumqi 830063, China |
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Abstract: |
Walnut protein is a high-quality vegetable protein, but its low solubility limits its application in food. In order to broaden the application scope of walnut protein, different proteases (alkaline protease, pepsin, trypsin, papain, neutral protease) were used to hydrolyze walnut protein isolate, and then the degree of hydrolysis, secondary structures and functionality (solubility,water absorption, oil absorption, emulsification and foaming properties) of different hydrolysates were determined. The results showed that the degree of hydrolysis of alkaline protease (22.16%) was the highest, following that of papain (20.06%), while the degree of hydrolysis of trypsin (13.95%) was the lowest. FTIR results exhibited that the secondary structures of the five hydrolysates were mainly β-sheet and β-turn. At pH 7.0,compared with the water absorption (2.36 g/g) and oil absorption (4.65 g/g) of walnut protein isolate without enzymatic hydrolysis, the different hydrolysates increased by 11.58-17.15 g/g and 7.58-15.44 g/g, respectively; at different pH (2-12), the solubility of the enzymatic hydrolysates significantly increased; at different pH and NaCl concentration, the emulsification and foaming properties of the enzymatic hydrolysates were different. From the perspective of improving protein functionality, alkaline protease is the best enzyme for hydrolysis of walnut protein isolate. |
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