New plant endopeptidases with potential aplication in chesemaking

PARDO M.F; BRUNO M.A.; SEQUEIROS C.; TREJO S.A.,; LÓPEZ L.M.I.; CAFFINI N.O. ; NATALUCCI CL.

ACTA ALIMENTARIA (BUDAPEST)

AKADEMIAI KIADO RT

Lugar: Budapest; Año: 2010 vol. 39 p. 200 - 210

0139-3006

Results are given on the milk clotting properties and casein hydrolytic behaviour of partially purified extracts of four new cysteine plant endopeptidases: balansain, hieronymain, asclepain f, and philibertain g. Milk coagulation behaviour was different for the assayed proteases: balansain and hieronymain showed a similar performance, whereas asclepain f exhibited the lowest clotting activity; philibertain g exhibited the highest one when was previously incubated with cysteine. According to the relative ratio of clotting activity to proteolytic activity, balansain, philibertain g and hieronymain appear as possible vegetable rennets. Casein hydrolysates were produced with each enzyme and the hydrolysis pattern was analysed by tricine SDS-PAGE. The áS2- and áS1-casein fractions, associated with cheese texture, showed different degradation patterns: higher degradation kinetics was obtained for philibertain g, followed by balansain and hieronymain, whereas asclepain f showed the lowest activity. The â-casein fraction, related to bitterness, showed similar initial degradation kinetics for balansain and asclepain f; degradation was faster in the case of philibertain g and slower for hieronymain. In the case of the ê-casein fraction, involved in milk clotting, the most remarkable behaviour was that of hieronymain, as this casein fraction was quickly degraded by the protease.S2- and áS1-casein fractions, associated with cheese texture, showed different degradation patterns: higher degradation kinetics was obtained for philibertain g, followed by balansain and hieronymain, whereas asclepain f showed the lowest activity. The â-casein fraction, related to bitterness, showed similar initial degradation kinetics for balansain and asclepain f; degradation was faster in the case of philibertain g and slower for hieronymain. In the case of the ê-casein fraction, involved in milk clotting, the most remarkable behaviour was that of hieronymain, as this casein fraction was quickly degraded by the protease.