Einfluß der enzymatischen Modifizierung auf die Lysinoalaninbildung in Ackerbohnenproteinisolat und β‐Casein

Abstract

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.

Untersuchungen zum Emulgierverhalten von enzymatisch modifiziertem Ackerbohnenproteinisolat

“…Die Herstellung der peptischen und thermitatischen API-Partialhydrolysate (PH) wurde bereits beschrieben [21]. Die rnit Brauereienzym erzeugten PH wurden analog bei pH 6,9 ( I N Natronlauge) und 45 -C gewonnen; jedoch betrug das Enzym-Substrat-Verhaltnis 4.8 : 100 in 6 "/,iger Proteinsuspcnsion.…”