A sequence-specific nicking endonuclease from streptomyces: purification, physical and catalytic properties.

A sequence-specific nicking endonuclease from Streptomyces designated as DC13 was purified to near homogeneity. Starting with 30 grams of wet cells, the enzyme was purified by ammonium sulfate fractionation, DEAE cellulose, and phenyl-Sepharose chromatography. The purified protein had a specific activity 1000 units/mg and migrated on SDS-PAGE gel with an estimated molecular weight of 71 kDa.

Cloning of a thermostable xylanase from Actinomadura sp. S14 and its expression in Escherichia coli and Pichia pastoris.

A thermophilic xylan-degrading Actinomadura sp. S14 was isolated from compost in Thailand. Hemicellulase activities such as endo-1,4-β-xylanase, β-xylosidase and α-arabinofuranosidase were induced with xylan-containing agriculture wastes and oat spelt xylan.

Involvement of PEG-carboxylate dehydrogenase and glutathione S-transferase in PEG metabolism by Sphingopyxis macrogoltabida strain 103.

Sphingopyxis terrae and the Sphingopyxis macrogoltabida strains 103 and 203 are able to degrade polyethylene glycol (PEG). They possess the peg operon, which is responsible for the conversion of PEG to PEG-carboxylate-coenzyme A (CoA). The upstream (3.

Polyethylene glycol (PEG)-carboxylate-CoA synthetase is involved in PEG metabolism in Sphingopyxis macrogoltabida strain 103.

Sphingopyxis macrogoltabida strain 103 possesses polyethylene-glycol (PEG)-inducible pegBCDAE operon encoding the genes relevant to PEG degradation. PEG is converted to PEG-carboxylate by PegA (PEG dehydrogenase) and PegC (PEG-aldehyde dehydrogenase). In this study, the recombinant PegE (homologous to acyl-CoA synthetases) was characterized.