The interaction mechanism and the functionality of yeast protein with hydrophilic and hydrophobic bioactive molecules  

作　　者：Haili Sun Yifei Sun Xin Tang Yuanmeng Cui Demei Meng Yuyu Zhang Ku Li Hui Guo Hai Chen Rui Yang 

机构地区：[1]State Key Laboratory of Food Nutrition and Safety,College of Food Science and Engineering,Tianjin University of Science&Technology,Tianjin,300457,China [2]Beijing Key Laboratory of Flavor Chemistry,Beijing Technology and Business University(BTBU),Beijing,100048,China [3]Angel Yeast Co.LTD.,Hubei,China [4]College of Food Science,Southwest University,Chognqing,400715,China

出　　处：《Food Bioscience》2023年第2期990-999,共10页食品生物科学（英文）

基　　金：This work was supported by the Natural Science Foundation of Tianjin City,China(No.20JCYBJC00020);the National Natural Science Foundation of China(No.31972067);the Beijing Outstanding Young Scientist Program(BJJWZYJH01201910011025);the fund from Key Technology of Biological Manufacturing of Yeast Products with Salt reduction and Flavor Enhancement(No.2020ZYYD028);the Project Program of Key Laboratory of Tianjin Key Laboratory of Food Quality and Health,China(No.TJS202203).

摘　　要：Yeast protein is a kind of yeast-source high-quality complete protein.The coexistence of bioactive molecules with yeast protein may influence its physicochemical property.This study discussed the interaction mechanism of yeast protein with two bioactive molecules,the hydrophobic curcumin and the hydrophilic epigallocatechin gallate(EGCG).Results indicated that curcumin and EGCG could interact with yeast protein with different binding stoichiometric numbers(0.8109±0.0695 and 2.7248±0.2422)and binding constants((3.8152±0.0078)×10^(4) and(1.1875±0.0440)×10^(5)),respectively.Both EGCG and curcumin decreased theα-helix content while increased theβ-sheet proportion,and co-binding remarkably reduced theα-helix proportion relative to the single ligand binding.The co-binding of these two compounds decreased the association extent of the yeast protein,which in turn reduced the diameter of yeast protein-EGCG-curcumin complex.The binding of EGCG with yeast protein improved the thermal stability of curcumin.Moreover,the co-binding improved the emulsification stability of yeast protein,and curcumin exhibited a more remarkable effect in improving the foamability.This work provides a theoretical basis for clarifying the interaction mechanisms of hydrophobic/hydrophilic molecules with yeast protein,and extends the potential applications of the novel fungus protein sources for food function enhancement and bioactive molecule stabilization.

关 键 词：Yeast protein Bioactive ligands Non-covalent binding Stability EMULSIFICATION 

分 类 号：TS201[轻工技术与工程—食品科学]