Ability of various proteins to form thermostable gels with propylene glycol alginate

Propylene glycol alginate forms gels with proteins in alkaline conditions (pH 9.3 to 10.5). The ability of gelatin, casein, soya isolate, whey protein concentrate, egg albumin and bovine serum albumin to form ‘protein-alginate’ gels was investigated. Conditions were varied so as to alter the structu...

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Main Authors: Mohamed, Suhaila, Stainsby, George
Format: Article
Language:English
Published: Elsevier 1984
Online Access:http://psasir.upm.edu.my/id/eprint/36855/
http://psasir.upm.edu.my/id/eprint/36855/1/36855.pdf
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author Mohamed, Suhaila
Stainsby, George
author_facet Mohamed, Suhaila
Stainsby, George
author_sort Mohamed, Suhaila
building UPM Institutional Repository
collection Online Access
description Propylene glycol alginate forms gels with proteins in alkaline conditions (pH 9.3 to 10.5). The ability of gelatin, casein, soya isolate, whey protein concentrate, egg albumin and bovine serum albumin to form ‘protein-alginate’ gels was investigated. Conditions were varied so as to alter the structures of the protein and observe the effect on gel formation. These conditions include changing pH, heat, the action of nitrous acid, SDS, mercaptoethanol, hydrogen bond breakers and changing concentration of the protein. The extent of gel formation was indicated by its rigidity modulus. The tertiary structure of the protein appears to be a very important factor in the gel formation. The gels are readily brought down to pH values more suitable for foods, and are stable to heating at 95°C and to freeze-thawing.
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spelling upm-368552016-02-01T05:02:34Z http://psasir.upm.edu.my/id/eprint/36855/ Ability of various proteins to form thermostable gels with propylene glycol alginate Mohamed, Suhaila Stainsby, George Propylene glycol alginate forms gels with proteins in alkaline conditions (pH 9.3 to 10.5). The ability of gelatin, casein, soya isolate, whey protein concentrate, egg albumin and bovine serum albumin to form ‘protein-alginate’ gels was investigated. Conditions were varied so as to alter the structures of the protein and observe the effect on gel formation. These conditions include changing pH, heat, the action of nitrous acid, SDS, mercaptoethanol, hydrogen bond breakers and changing concentration of the protein. The extent of gel formation was indicated by its rigidity modulus. The tertiary structure of the protein appears to be a very important factor in the gel formation. The gels are readily brought down to pH values more suitable for foods, and are stable to heating at 95°C and to freeze-thawing. Elsevier 1984 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/36855/1/36855.pdf Mohamed, Suhaila and Stainsby, George (1984) Ability of various proteins to form thermostable gels with propylene glycol alginate. Food Chemistry, 13 (4). pp. 241-255. ISSN 0308-8146 http://www.sciencedirect.com/science/article/pii/0308814684900888 10.1016/0308-8146(84)90088-8
spellingShingle Mohamed, Suhaila
Stainsby, George
Ability of various proteins to form thermostable gels with propylene glycol alginate
title Ability of various proteins to form thermostable gels with propylene glycol alginate
title_full Ability of various proteins to form thermostable gels with propylene glycol alginate
title_fullStr Ability of various proteins to form thermostable gels with propylene glycol alginate
title_full_unstemmed Ability of various proteins to form thermostable gels with propylene glycol alginate
title_short Ability of various proteins to form thermostable gels with propylene glycol alginate
title_sort ability of various proteins to form thermostable gels with propylene glycol alginate
url http://psasir.upm.edu.my/id/eprint/36855/
http://psasir.upm.edu.my/id/eprint/36855/
http://psasir.upm.edu.my/id/eprint/36855/
http://psasir.upm.edu.my/id/eprint/36855/1/36855.pdf