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Evaluation of the binding affinity and antioxidant activity of phlorizin to pepsin and trypsin

作     者:Jing Zhang Lan Tang Xia Hu Zhen Zeng Wen Wu Fang Geng Hui Li Di Wu Jing Zhang;Lan Tang;Xia Hu;Zhen Zeng;Wen Wu;Fang Geng;Hui Li;Di Wu

作者机构:Meat Processing Key Laboratory of Sichuan ProvinceSchool of Food and Biological EngineeringChengdu UniversityChengdu 610106China School of Chemical EngineeringSichuan UniversityChengdu 610065China 

出 版 物:《Food Science and Human Wellness》 (食品科学与人类健康(英文))

年 卷 期:2024年第13卷第1期

页      面:392-400页

核心收录:

学科分类:0832[工学-食品科学与工程(可授工学、农学学位)] 08[工学] 083201[工学-食品科学] 

基  金:supported by the National Natural Science Foundation of China(21808020) the Applied Basic Research Program of Science&Technology Department of Sichuan Province(2018JY0151) 

主  题:Interaction Phlorizin Pepsin Trypsin Antioxidation 

摘      要:Phlorizin(PHL)is a natural compound with strong antioxidant properties mainly found in *** this paper,the interaction mechanism of PHL with pepsin and trypsin was comparatively evaluated by computer simulation,fluorescence spectra,circular dichroism(CD),and Fourier transform infrared(FT-IR)spectra at a molecular *** spectra showed that PHL quenches the pepsin/trypsin by static *** parameters indicated that PHL binds to pepsin mainly through hydrogen bonds and van der Waals forces,and that of trypsin was electrostatic *** ground state complexes PHL and protease have a moderate affinity of 105 L/mol PHL binds more strongly to trypsin than to *** and FT-IR spectra results showed that pepsin/trypsin decreased theβ-sheet content and slightly changed its secondary structure upon *** experimental results are mutually verified with the predicted computer-aid simulation *** PHL and trypsin binding,the antioxidant capacity of PHL was ***,the antioxidant capacity of PHL was decreased after binding to *** work elucidates the binding of PHL binding mechanisms to pepsin/trypsin and provides useful information for the digestion of PHL to improve the application of PHL in food processing.

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