NDLI: Characterization of a β-glycosidase from the thermoacidophilic bacterium Alicyclobacillus acidocaldarius

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Characterization of a β-glycosidase from the thermoacidophilic bacterium Alicyclobacillus acidocaldarius

Content Provider	Springer Nature Link
Author	Lauro, Barbara Di Rossi, Mosè Moracci, Marco
Copyright Year	2006
Abstract	In cell free extracts of the thermoacidophilic gram-positive bacterium Alicyclobacillus acidocaldarius ATCC27009, we have identified β-gluco- and galactosidase activities showing a specific activity of 0.1 and 12 U/mg, respectively. The two enzymatic activities are associated with different polypeptides and we show here the functional cloning, the expression in Escherichia coli and the characterisation of the β-glucosidase (Aaβ-gly). The enzyme, which is optimally active and stable at temperatures above 65°C, belongs to glycoside hydrolase family 1 (GH1) and shows wide substrate specificity on different aryl-glycosides and cello-oligosaccharides with k cat/K M for 4-nitrophenyl-β-D-glucoside and cellobiose of 2,976 and 185 s−1mM−1, respectively. Interestingly, upstream to the β-glycosidase gene, we identified a second ORF homologous to the ATPase subunit of the bacterial ABC transporters (abc1) that is co-transcribed with the β-glycosidase gene glyB and that could be involved in the carbohydrate import. The activity of the enzyme on cello-oligosaccharides of up to five glucose units strongly indicates that the enzyme could be involved in vivo in the degradation of glucans together with endoglucanase enzymes previously described. This, together with the co-expression of the two genes, suggests a role for the glyB-abc1 cluster in A. acidocaldarius in the degradation of cellulose and hemicelluloses.
Starting Page	301
Ending Page	310
Page Count	10
File Format	PDF
ISSN	14310651
Journal	Extremophiles
Volume Number	10
Issue Number	4
e-ISSN	14334909
Language	English
Publisher	Springer-Verlag
Publisher Date	2006-04-12
Publisher Place	Tokyo
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Thermophilic enzymes Acidophiles Cellulose degradation Recombinant enzymes Gene expression Ecology Biotechnology Microbiology
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Medicine Microbiology

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Characterization of a β-glycosidase from the thermoacidophilic bacterium Alicyclobacillus acidocaldarius

Characterization of a β-glycosidase from the thermoacidophilic bacterium Alicyclobacillus acidocaldarius

Irreversible inhibition of the thermophilic esterase EST2 from Alicyclobacillus acidocaldarius

Heterologous expression and characterization of a malathion-hydrolyzing carboxylesterase from a thermophilic bacterium, Alicyclobacillus tengchongensis

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Hydrolysis and Transglycosylation Activity of a Thermostable Recombinant β-Glycosidase from Sulfolobus acidocaldarius

Heterologous expression of a gene encoding a thermostable β-galactosidase from Alicyclobacillus acidocaldarius

Enlarging the substrate portfolio of the thermophilic esterase EST2 from Alicyclobacillus acidocaldarius

Modification of the enantioselectivity of two homologous thermophilic carboxylesterases from Alicyclobacillus acidocaldarius and Archaeoglobus fulgidus by random mutagenesis and screening

Characterization of a β-glycosidase from the thermoacidophilic bacterium Alicyclobacillus acidocaldarius

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Characterization of a β-glycosidase from the thermoacidophilic bacterium Alicyclobacillus acidocaldarius