4.7 Article

Characteristics of soy protein hydrolysate nanofibrils and their stabilization mechanism for Pickering emulsion: Interfacial properties, Rheology and stability

Journal

LWT-FOOD SCIENCE AND TECHNOLOGY
Volume 189, Issue -, Pages -

Publisher

ELSEVIER
DOI: 10.1016/j.lwt.2023.115473

Keywords

Enzymatic hydrolysis; Soy protein; Nanofibrils; Pickering emulsion; Stability

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Enzymatic hydrolysis of soy protein isolate improves its physicochemical properties and enhances its application in stabilizing Pickering emulsion. This study investigates the effects of enzymatic hydrolysis on the fibrillation of soy protein isolate and the mechanisms behind the stabilization of Pickering emulsion by SPI hydrolysate nanofibrils. The results show that SPI hydrolysate can form long and flexible nanofibrils with improved stability in Pickering emulsion.
Enzymatic hydrolysis is an effective method to improve the physicochemical properties of soy protein isolate (SPI) nanofibrils and expand their application in stabilizing Pickering emulsion. In this work, the effects of enzymatic hydrolysis on the SPI fibrillation and the stabilization mechanisms of SPI hydrolysate nanofibrils for Pickering emulsion were investigated. According to sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) images and Thioflavin T (ThT) fluorescence data, a higher degree of hydrolysis (DH) contributed to releasing more small molecular weight peptides (mainly from alpha, alpha ', and beta subunits) to improve apparent rate constant and surface hydrophobicity during fibrillation. When DH increased to 8%, SPI hydrolysate could form long and flexible nanofibrils and possessed the highest content of beta-sheet (21.40%), when heated for 12 h. Enzymatic hydrolysis played various positive impacts on the interfacial properties of nanofibrils, including faster interfacial adsorption and near-neutral wettability (92.87 degrees). SPI hydrolysate nanofibrils could impart enhanced gel-like structure and exceptional thermal stability to Pickering emulsions, resulting in a decrease in droplet size from 52.06 mu m to 32.74 mu m. This work will enhance the exploration of the formation mechanism of nanofibrils and broaden their application in the functional emulsion.

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