2008 journal article

Molecular interactions and functionality of a cold-gelling soy protein isolate

JOURNAL OF FOOD SCIENCE, 73(1), E16–E24.

By: G. Cramp n, P. Kwanyuen n & C. Daubert n

author keywords: cold-gelling; critical concentration; disulfide bonds; hydrophobic interactions; soy protein isolate
MeSH headings : Calorimetry, Differential Scanning; Chemical Phenomena; Chemistry, Physical; Cold Temperature; Electrophoresis, Agar Gel; Food Handling / methods; Gels; Protein Denaturation; Rheology; Soybean Proteins / analysis; Soybean Proteins / chemistry; Time Factors; Viscosity
TL;DR: The results suggested that heat denaturation at low protein concentrations limited network formation even after the protein concentration and interaction sites increased, impacting the isolate's cold gelling ability and suggested that hydrophobic interactions played a primary role in gel strength after disulfide bonds form. (via Semantic Scholar)
UN Sustainable Development Goal Categories
Source: Web Of Science
Added: August 6, 2018

Citation Index includes data from a number of different sources. If you have questions about the sources of data in the Citation Index or need a set of data which is free to re-distribute, please contact us.

Certain data included herein are derived from the Web of Science© and InCites© (2024) of Clarivate Analytics. All rights reserved. You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.