HEAT INDUCED GELS FROM PARTIALLY HYDROLYZED SOY PROTEIN ISOLATE

Autor:	M. A. Hanna, L. D. Satterlee, E. J. Garcia Chacon
Rok vydání:	1990
Předmět:	Pharmacology chemistry.chemical_classification Chromatography Chemistry Size-exclusion chromatography Biophysics Proteolytic enzymes Peptide Cell Biology Electrophoresis Biochemistry Sephadex Plant protein Solubility Soy protein Food Science
Zdroj:	Journal of Food Biochemistry. 14:15-29
ISSN:	1745-4514 0145-8884
DOI:	10.1111/j.1745-4514.1990.tb00818.x
Popis:	Heat induced gels can be obtained from partially hydrolyzed soy protein isolate (HSPI). The gel forming ability of each of the HSPI fractions (peptides of varying molecular weight and solubility) were studied, after being separated by preparative Sephadex gel filtration chromatography. The insoluble peptide fraction had no gel forming ability. Peptides larger than 5,000 Daltons, those lower than 5,000 Daltons and a fraction of the very hydrophobic peptides formed weak gels when heated alone. Interactions between several peptide fractions were necessary in order to yield a gel with the strength of the one formed by whole HSPI. A mechanism explaining (1) the action of the proteolytic enzyme in breaking down the protein and (2) the peptide interaction needed for the gel formation, is proposed.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::c689519814f7f9f84e05087da8a8cc5a https://doi.org/10.1111/j.1745-4514.1990.tb00818.x Zobrazit plný text záznamu