Crystal structure of the catalytic domain of a GH16 β-agarase from a deep-sea bacterium, Microbulbifer thermotolerans JAMB-A94.

A deep-sea bacterium, Microbulbifer thermotolerans JAMB-A94, has a β-agarase (MtAgaA) belonging to the glycoside hydrolase family (GH) 16. The optimal temperature of this bacterium for growth is 43-49 °C, and MtAgaA is stable at 60 °C, which is one of the most thermostable enzymes among GH16 β-agarases. Here, we determined the catalytic domain structure of MtAgaA.

alpha-Glucosidase from a strain of deep-sea Geobacillus: a potential enzyme for the biosynthesis of complex carbohydrates.

An alpha-glucosidase from Geobacillus sp. strain HTA-462, one of the deepest sea bacteria isolated from the sediment of the Mariana Trench, was purified to homogeneity and estimated to be a 65-kDa protein by SDS-PAGE. At low ion strength, the enzyme exists in the homodimeric form (130 kDa).

A novel beta-glucanase gene from Bacillus halodurans C-125.

A novel endo-beta-1,3(4)-D-glucanase gene was found in the complete genome sequence of Bacillus halodurans C-125. The gene was previously annotated as an "unknown" protein and assigned an incorrect open reading frame (ORF). However, determining the biochemical characteristics has elucidated the function and correct ORF of the gene.

Crystallization and preliminary X-ray study of alkaline mannanase from an alkaliphilic Bacillus isolate.

An alkaline mannanase (EC 3.2.1.

Crystallization and preliminary X-ray study of gamma-type cyclodextrin glycosyltransferase from Bacillus clarkii.

A gamma-cyclodextrin glycosyltransferase (EC 2.4.1.

Crystallization and preliminary X-ray study of isomaltodextranase from Arthrobacter globiformis.

A recombinant isomaltodextranase (1,6-alpha-D-glucan isomaltohydrolase; EC 3.2.1.

Crystallization and preliminary X-ray study of alpha-glucosidase from Geobacillus sp strain HTA-462, one of the deepest sea bacteria.

An alpha-glucosidase (EC 3.2.1.