New plant endopeptidases with potential application in cheesemaking

Pardo, M. and Bruno, M. and Sequeiros, C. and Trejo, S. and López, L. and Caffini, N. and Natalucci, C. (2010) New plant endopeptidases with potential application in cheesemaking. Acta Alimentaria, 39 (2). pp. 211-221. ISSN 0139-3006

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Abstract

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 α S2 - and α S1 -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 β-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 κ-casein fraction, involved in milk clotting, the most remarkable behaviour was that of hieronymain, as this casein fraction was quickly degraded by the protease.

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