THE FORMATION OF HEAT AND ENZYME INDUCED (PLASTEIN) GELS FROM PEPSIN-HYDROLYZED SOY PROTEIN ISOLATE

Autor:	L. D. Satterlee, E. K. Hartnett
Rok vydání:	1990
Předmět:	Pharmacology Chromatography Protease biology medicine.medical_treatment Biophysics Cell Biology Papain chemistry.chemical_compound Hydrolysis chemistry Pepsin Plant protein biology.protein medicine Peptide bond Solubility Soy protein Food Science
Zdroj:	Journal of Food Biochemistry. 14:1-13
ISSN:	1745-4514 0145-8884
DOI:	10.1111/j.1745-4514.1990.tb00817.x
Popis:	A gel prepared by heating pepsin-hydrolyzed soy protein isolate (HSPI) had a higher turbidity and viscosity and less solubility than did its starting hydrolyzate. The gelling characteristics of the heated hydrolyzate were possibly due to hydrophobic interactions, as opposed to peptide bond reformation. The presence of pepsin was found to be necessary for gel formation at 37°C but could be successfully replaced by heat. Incubation of the concentrated HSPI at 95°C for 30 min was optimal for heat-induced gel formation. When soy protein isolate (SPI) was hydrolyzed with papain or bacterial protease, little gelation occurred (either by heat or enzyme induced gelation treatments).
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::620655604b303526f2b4126e5f9c0f5e https://doi.org/10.1111/j.1745-4514.1990.tb00817.x Zobrazit plný text záznamu