Purification and characterization of microbial gellan lyase
Article Abstract:
Gellan lyase can be purified from a medium with gellan, an exopolysaccharide formed by Sphingomonas paucimobilis, as the only carbon source. The enzyme is a monomer, has a molecular mass of 140 kDa and optimum conditions for activity are pH 7.5 and 45 degrees Centigrade. The enzyme is specific for gellan and lowers its viscosity. Gellan lyase can be used to make a polysaccharide with a gellan backbone that has applications in food technology and polymer-based industries.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1996
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Characterization and molecular cloning of a novel enzyme, inorganic polyphosphate/ATP-glucomannokinase, of Arthrobacter sp. strain KM
Article Abstract:
Results show that inorganic polyphosphate/ATP-glucomannokinase from Arthrobacter sp. strain KM is a monomer with a molecular mass of 30 kilodalton and phosphorylates glucose and mannose using poly(P) and ATP. The gene encoding the enzyme contains an open reading frame of 804 base pairs and the amino acid sequence shows 45% homology to that of Mycobacterium tuberculosis H37Rv poly(P)/ATP-glucokinase.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2003
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NADP(H) phosphatase activities of archael inositol monophosphatase and eubacterial 3'-phosophoadenosine 5'-phosphate phosphatase
Article Abstract:
The NADP(H) phosphatase-activities of several archael inositol monophosphatases and eubacterial 3'-phosphoadenosine 5'-phosphate phosphatase (CysQ) are studied. The results show that CysQ functions physiologically as 3'-phosphoadenosine 5'-phosphate phosphatase rather than NADP(H) phosphatase.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2007
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