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Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders
Published on: April 14, 2015
Structure regulation mechanisms and interfacial properties of soy protein isolate with pH and heat treatment
Jiaying Chen1, Mingxia Pu1, Yilin Wang1
1Department of Food Science and Pharmaceutics, Zhejiang Ocean University, Zhoushan 316022, China.
Abstract:
This study investigated the assembly mechanisms, interfacial properties, and structure-function relationships of soybean protein isolate (SPI) via the synergistic effects of pH regulation and heat treatment. Two molten globular (SPG), three aggregated (SPA), and one fibrous (SPF) SPI conformations were successfully prepared. SPG had reduced random coil content; among them, SPG-12 showed the highest solubility (71.6%) and lowest surface hydrophobicity (5025), thus exhibiting optimal emulsifying and foaming properties. Heat induction and pH cycling enhanced SPI solubility and promoted the formation of nanoparticles smaller than 200 nm, while isoelectric point-induced aggregation inhibited ordered structures (e.g., SPA-2 with particle size over 500 nm). SPF formed through three steps: unfolding, then hydrolysis, and finally aggregation; during this process, disulfide bond content first dropped from 63.4% to 32.2% and then recovered to 64.1%, and SPF had improved foaming capacity but reduced stability. This work provides theoretical support for developing plant-based emulsifiers and foaming agents.
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