Purification and Characterization of an Intracellular [beta]-Glucosidase from Lactobacillus casei ATCC 393

The lactic acid bacterium,Lactobacillus casei, produces an intracellular β-glucosidase when grown on Man-Rogosa-Sharpe (MRS) medium with cellobiose as carbon source. The β-glucosidase activity is produced intracellulary, and no extracellulary activity was detected. The enzyme was purified by ion-exc...

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Bibliographic Details
Published in:Applied biochemistry and biotechnology 1998-08, Vol.74 (2), p.105
Main Authors: Coulon, S, Chemardin, P, Gueguen, Y, Arnaud, A, Galzy, P
Format: Article
Language:English
Subjects:
Bacteria
Biotechnology
Carbon sources
Chromatography
Enzymes
Ethanol
Filtration
Online Access:Get full text
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Summary:The lactic acid bacterium,Lactobacillus casei, produces an intracellular β-glucosidase when grown on Man-Rogosa-Sharpe (MRS) medium with cellobiose as carbon source. The β-glucosidase activity is produced intracellulary, and no extracellulary activity was detected. The enzyme was purified by ion-exchange chromatography and gel filtration. The molecular mass of the purified intracellular β-glucosidase as estimated by gel filtration was 480 kDa, consisting of six probably identical subunits. The enzyme exhibited optimum activity at 35°C and pH 6.3 with citrate-phosphate buffer. The enzyme was active against soluble glycosides with (1[arrow right]4)-β configuration and from Lineweaver Burk plots, K^sub m^ value of 16 mmol/L was found for β-pNPG. The β-glucosidase was competitively inhibited by glucose, and no glycosyl transferase activity was observed in the presence of ethanol.[PUBLICATION ABSTRACT]
ISSN:0273-2289
1559-0291
DOI:10.1007/BF02787177