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J. Dairy Sci. 87:1132-1142
© American Dairy Science Association, 2004.

Purification and Characterization of a Pregastric Esterase From a Hygienized Kid Rennet Paste

M. V. Calvo and J. Fontecha

Dpto. de Ciencia y Tecnología de Productos Lácteos, Instituto del Frío (CSIC), C/José Antonio Novais, 10 Ciudad Universitaria, 28040 Madrid, Spain.

Corresponding author: M. V. Calvo; e-mail: mcalvo{at}if.csic.es.

Rennet pastes obtained by maceration of gastric tissues from suckling kids are used traditionally to produce some artisanal cheeses in Spain. Besides milk-clotting function, rennet pastes provide proteolytic activity and lipolytic system, essentially pregastric, necessary in the development of piquant flavor typical of these cheeses. A simple and reproducible procedure allows us to obtain a standardized rennet paste that posses the desired activity and is of good microbiological quality. Concomitantly, a kid pregastric esterase (KPGE) was purified to homogeneity. The purification procedure was based on an aqueous extract of hygienized rennet paste (HRP), which was chromatographed on DEAE-Sepharose Fast Flow then adsorbed on phenyl superose followed by a re-chromatography on the same column. The final enzymatic preparation, where the overall activity recovery was 3%, showed a molecular mass of 53 kDa. The highest activity was determined on p-nitrophenyl butyrate, but marked hydrolysis was also detected on ß-naphthyl caprylate. In contrast, low activity on tributyrin (substrate under emulsion form) was detected, thus confirming the esterase character of purified enzyme.

Key Words: rennet paste • pregastric esterase • artisanal cheese

Abbreviation key: KPGE = kid pregastric esterase, HRP = hygienized rennet paste, p-NPB = p-nitrophenyl butyrate, p-NPC = p-nitrophenyl caprylate, ß-NC = ß-naphthyl caprylate






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