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Molecular characterization of cycloinulooligosaccharide fructanotransferase from Bacillus macerans

Article Abstract:

The 358-residue region of the N-terminus of cycloinulooligosaccharide fructanotransferase from Bacillus macerans appears to be involved in binding to the inulin substrate. This enzyme catalyzes the intramolecular transfructosylation reaction that converts inulin into cyclooligosaccharides of beta-(2 to 1)-linked D-fructofuranose.

Author: Kim, Hwa-Young, Choi, Yong-Jin
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2001
Binding sites (Biochemistry), Active sites (Biochemistry)

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Characterization of a heme-dependent catalase from Methanobrevibacter arboriphilus

Article Abstract:

Researchers have isolated a heme-containing catalase from Methanobrevibacter arboriphilus that is produced form apoprotein synthesized by the bacterium and hemin present in the medium. The catalase is similar to the catalase produced by Methanosarcina barkeri.

Author: Shima, Seigo, Sordel-Klippert, Melanie, Brioukhanov, Andrei, Netrusov, Alexander, Linder, Dietmar, Thauer, Rudolf K.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2001
Hemoproteins

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Genetic and biochemical characterization of a highly thermostable alpha-L-arabinofuranosidase from Thermobacillus xylanilyticus

Article Abstract:

An alpha-L-arabinofuranosidase from Thermobacillus xylanilyticus D3 may belong to family 51 of the glycosyl hydrolase classification system. However, unlike most of the F51 members, it is highly active in the presence of polysaccharides.

Author: Debeche, Takoua, Cummings, Nicola, Connerton, Ian, Debeire, Philippe, O'Donohue, Michael J.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2000

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Subjects list: Research, Microbial enzymes
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