Abstract
The molten globule (MG) state of soy protein isolate (SPI) is an intermediate stage between the natural and denatured states, where the protein is undergoing unfolding. In this study, we investigated the conformational changes of SPI induced to form the MG state using polar acid (pH 1.0–3.0) and polar alkaline (pH 10.0–12.0) solutions. Our findings indicate that extreme pH treatment can induce the transformation of SPI into the MG state, resulting in a series of structural changes. Compared to SPI, the foaming capacity of the MG state improved by 77–113%, and foam stability improved by 60–124%, resulting in noticeably improved foaming characteristics. Similarly, the emulsification property and emulsification activity of MG state were remarkably enhanced. This study offers new understanding of the MG state of SPI and offers a theoretical basis for developing food, pharmaceutical, and cosmetic products with excellent foaming and emulsifying properties.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
