Characterization of a broad pH range protease of Candida caseinolytica

Poza, M.; Miguel, T. de; Sieiro, C.; Villa, T.G.

Characterization of a broad pH range protease of Candida caseinolytica

2001

Poza, M. | Miguel, T. de | Sieiro, C. | Villa, T.G.

Aims: The study of a protease secreted by Candida caseinolytica for use in future industrial applications. Methods and Results: Growth of Candida caseinolytica on a medium containing milk induced a rapid production of an extracellular enzyme able to hydrolyse casein. The crude extract was applied to both Sephacryl S-200 and DEAE-Biogel A columns, obtaining one peak of activity showing a molecular mass of approximately equal to 30 kDa and three active peaks, respectively. These four peaks showed the same biochemical parameters. In all cases, an extremely broad pH range of action was determined. Conclusions: Candida caseinolytica secretes high levels of an extracellular protease when grown either in rotary shakers or in batch-fermenters. Significance and Impact of the Study: The biochemical properties of this enzyme suggest its possible industrial application in the brewing industry, in the formulation of certain type of detergents and in the fur and leather industries, among others.

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