Mechanistic insights into the effects of controlled enzymatic hydrolysis on the binding behaviors between soy protein isolate and off-flavor compounds

Xuejie Li; Wentao Zhang; Meihong Yu; Haoxiang Tan; Xiangquan Zeng; Yu Xi; He Li; Zengwang Guo; Jian Li

doi:10.1016/j.foodchem.2024.142271

Mechanistic insights into the effects of controlled enzymatic hydrolysis on the binding behaviors between soy protein isolate and off-flavor compounds

Food Chem. 2024 Nov 26:467:142271. doi: 10.1016/j.foodchem.2024.142271. Online ahead of print.

Authors

Xuejie Li¹, Wentao Zhang¹, Meihong Yu¹, Haoxiang Tan¹, Xiangquan Zeng¹, Yu Xi¹, He Li¹, Zengwang Guo², Jian Li³

Affiliations

¹ Key Laboratory of Green and Low-carbon Processing Technology for plant-based Food of China National Light Industry Council, School of Food and Health, Beijing Technology and Business University, Beijing, 100048, PR China.; Beijing Technology and Business University, Key Laboratory of Geriatric Nutrition and Health, Ministry of Education, Beijing 100048, PR China.
² College of Food Science, Northeast Agricultural University, Harbin 150030, PR China.
³ Key Laboratory of Green and Low-carbon Processing Technology for plant-based Food of China National Light Industry Council, School of Food and Health, Beijing Technology and Business University, Beijing, 100048, PR China.; Beijing Technology and Business University, Key Laboratory of Geriatric Nutrition and Health, Ministry of Education, Beijing 100048, PR China.. Electronic address: lijian@btbu.edu.cn.

PMID: 39616770
DOI: 10.1016/j.foodchem.2024.142271

Abstract

Regulating volatile compounds release through protein structural modification can influence food sensory properties. This study investigated the effects of controlled enzymatic hydrolysis (CEH) on the release of off-flavor compounds identified in soybean protein isolate (SPI) and revealed its potential mechanism of influence. CEH treatment significantly reduced the release of aldehydes, particularly (E, E)-2,4-decadienal, by inducing the unfolding of SPI unfolding. This structural modification exposed additional binding sites, thereby increasing the affinity of SPI for aldehyde compounds and effectively limiting aldehyde volatility. Multi-spectroscopic techniques, surface hydrophobicity, and dynamic light scattering (DLS) analyses confirmed these structural changes. Isothermal titration calorimetry (ITC) analysis suggested that non-covalent interactions, dominated by hydrogen bonds and hydrophobic interactions, were the primary factors driving these changes, as further confirmed by molecular dynamics (MD) simulations and independent gradient model (IGM) analysis. Additionally, proteomics revealed that covalent binding, including Michael addition and Schiff base reactions, also influenced the aldehydes release.

Keywords: Controlled enzymatic hydrolysis; Flavor release; Interactions; Soy protein isolate; Structural alteration.