Role of C-terminal domain in a manganese-catalase from Geobacillus thermopakistaniensis.

Catalases catalyze the decomposition of hydrogen peroxide into water and oxygen. We have characterized two manganese-catalases from Geobacillus thermopakistaniensis, Cat and Cat-II, which exhibited significant variation in their sequence, structure and properties. There was only 23% sequence identity between the two.

Looking into a highly thermostable and efficient recombinant manganese-catalase from Geobacillusthermopakistaniensis.

Catalases, heme or non-heme, are catalysts that decompose hydrogen peroxide. Among them, non-heme or manganese-catalases have been studied from limited organisms. We report here heterologous production of a manganese-catalase, Cat-II, previously annotated as a hypothetical protein, from a thermophilic bacterium Geobacillus thermopakistaniensis.

Structural and functional analyses of a novel manganese-catalase from Bacillus subtilis R5.

Catalases catalyze the decomposition of hydrogen peroxide into water and oxygen. Limited reports are available on characterization of manganese-catalases. We describe here molecular cloning and expression in Escherichia coli of a putative manganese-catalase gene from mesophilic bacterium, Bacillus subtilis R5.

A highly stable manganese catalase from Geobacillus thermopakistaniensis: molecular cloning and characterization.

Catalases, heme or manganese, are efficient biocatalysts that split hydrogen peroxide into water and oxygen. We have cloned a manganese catalase from thermophilic bacterium, Geobacillus thermopakistaniensis, and expressed the corresponding gene in Escherichia coli. The gene product, Cat, was synthesized in E.

A highly active α-cyclodextrin preferring cyclomaltodextrinase from Geobacillus thermopakistaniensis.

Cyclomaltodextrinases show diverse hydrolyzing and/or transglycosylation activities against cyclodextrins, starch and pullulan. A gene annotated as cyclomaltodextrinase from Geobacillus thermopakistaniensis was cloned and overexpressed in Escherichia coli. The gene product, CDase, was purified and biochemically characterized.