[The effect of enzymatic modification on lysinoalanine formation in field-bean protein isolate and beta-casein].
Lysinoalanine (LAL) was determined in alkali-treated partial hydrolysates (PH) of casein, peptides isolated from these PH and in PH of field-bean protein to clarify whether intermolecular or intramolecular LAL bridges are preferentially formed. Furthermore, the formation of LAS in plasteins was studied as a contribution to plastein research. The formation of LAL in the peptide mixtures of beta-casein and the decrease of the LAL content in the PH (as compared to intact proteins) indicates that the formation of LAL favours the intramolecular cross-linking of polypeptide chains. The LAL content decreases as the degree of hydrolysis of the PH of the field-bean protein isolate increases, and depends upon the protease used in the production of the hydrolysates. The LAL contents of the alkali-treated plasteins are less than those of the initial hydrolysates. The decrease of the LAL content is directly proportional to the hydrolysis proceeding during the plastein reaction.
D000596:Amino Acids / Q000032:analysis; D002364:Caseins / Q000032:analysis*; D004044:Dietary Proteins / Q000032:analysis*; D004220:Disulfides / Q000032:analysis; D007887:Fabaceae; D008239:Lysine / Q000031:analogs & derivatives*; D008241:Lysinoalanine / Q000032:analysis*; D010940:Plant Proteins / Q000032:analysis*; D010946:Plants, Medicinal; D011492:Protein Hydrolysates / Q000032:analysis*; D012995:Solubility; D014357:Trypsin
D000596:Amino Acids; D002364:Caseins; D004044:Dietary Proteins; D004220:Disulfides; D010940:Plant Proteins; D011492:Protein Hydrolysates; D008241:Lysinoalanine; D014357:Trypsin; D008239:Lysine
Einfluss der enzymatischen Modifizierung auf die Lysinoalaninbildung in Ackerbohnenproteinisolat und beta-Casein.