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Grace L. Cramp

Works (1)

Updated: July 5th, 2023 15:54

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
topics (OpenAlex): Proteins in Food Systems; Microencapsulation and Drying Processes; Protein Hydrolysis and Bioactive Peptides
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)
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Source: Web Of Science
Added: August 6, 2018

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