Autor:	Yves Popineau, B. Chaufer, Serge Bérot, Philippe Evon
Rok vydání:	1998
Předmět:	Hydrolysis Membrane Chromatography biology Chemistry Ultrafiltration biology.protein Fractionation Gliadin Gliadin peptide Hydrolysate
Zdroj:	Plant Proteins from European Crops ISBN: 9783662037225
DOI:	10.1007/978-3-662-03720-1_48
Popis:	Gliadin was hydrolyzed by α-chymotrypsin in 17 kg/mol peptides differing in their hydrophobicity and electrical charge. These peptides were separated on ultrafiltration membranes at acidic pH. Permeates contained 80 to 96% of neutral peptides, and retentates, which contained 80% of charged peptides, exhibited good emulsifying properties.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::bd35176458bae45fe28ae15c87b47b46 https://doi.org/10.1007/978-3-662-03720-1_48 Zobrazit plný text záznamu