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Purification and characterization of a pregastric esterase from a hygienized kid rennet paste

AutorCalvo, M. V.; Fontecha, F. Javier
Palabras claveRennet paste
Pregastric esterase
Artisanal cheese
Fecha de publicación2004
EditorAmerican Dairy Science Association
CitaciónJournal of Dairy Science 87: 1132- 1142 (2004)
ResumenRennet 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 β-naphthyl caprylate. In contrast, low activity on tributyrin (substrate under emulsion form) was detected, thus confirming the esterase character of purified enzyme.
Identificadoresdoi: 10.3168/jds.S0022-0302(04)73261-0
issn: 0022-0302
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