Literature DB >> 11722670

Characterization of a broad pH range protease of Candida caseinolytica.

M Poza1, T de Miguel, C Sieiro, T G Villa.   

Abstract

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 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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Year:  2001        PMID: 11722670     DOI: 10.1046/j.1365-2672.2001.01458.x

Source DB:  PubMed          Journal:  J Appl Microbiol        ISSN: 1364-5072            Impact factor:   3.772


  2 in total

1.  Production and characterization of the milk-clotting protease of Myxococcus xanthus strain 422.

Authors:  M Poza; C Sieiro; L Carreira; J Barros-Velázquez; T G Villa
Journal:  J Ind Microbiol Biotechnol       Date:  2003-11-22       Impact factor: 3.346

2.  Molecular Cloning and Optimization for High Level Expression of Cold-Adapted Serine Protease from Antarctic Yeast Glaciozyma antarctica PI12.

Authors:  Norsyuhada Alias; Mu'adz Ahmad Mazian; Abu Bakar Salleh; Mahiran Basri; Raja Noor Zaliha Raja Abd Rahman
Journal:  Enzyme Res       Date:  2014-06-30
  2 in total

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