Purification and characterization of the Bacillus subtilis levanase produced in Escherichia coli

Article Abstract:

The enzyme levanase produced by Bacillus subtilis is a beta-D-fructofuranosidase which hydrolyzes levan, inulin and sucrose. The molecular mass of the enzyme has been estimated to be 75,000 Da and it is most active at 5.5 pH and 55 degrees centigrade. The levanase breaks down inulin by the single-chain mechanism and a sulfhydral group is involved because in the presence of metal ions such as Ag+ and Hg2+, the enzyme does not breakdown any inulin.

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Isolation of methyl parathion-degrading strain M6 and cloning of the methyl parathion hydrolase gene

Article Abstract:

Researchers have isolated an organophosphate hydrolase from Plesiomonas sp. strain M6 that can convert methyl parathion to para-nitrophenol. The gene for this enzyme could be expressed in Escherichia coli and used to biodegrade organophosphate pesticides such as parathion, methyl parathion, and methamidophos.

Biodegradation, Organophosphorus compounds, Organic phosphorus compounds

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Purification and properties of an enzyme capable of degrading the sheath of Sphaerotilus natans

Article Abstract:

Researchers have discovered a bacterium which produces an enzyme that can degrade the sheath surrounding the bacterium Sphaerotilus natans. This enzyme could be useful in analyzing the structure of the sheath.

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