Microbial system for polysaccharide depolymerization: enzymatic route for xanthan depolymerization by Bacillus sp. strain GL1

Article Abstract:

An enzymatic route for the depolymerization of heteropolysaccharide xanthan in Bacillus sp. strain GL1, which was closely related to Brevibacillus thermoruber, was determined by analyzing the structures of xanthan depolymerization products. Tetrasaccharide was taken into cells and converted to a trisaccharide by beta-D-glucosidase, after which, it was converted to unsaturated glucuronic acid and a disaccharide by unsaturated glucuronyl hydrolase.

Polymerization, Xanthan gum

Xanthan lyase of Bacillus sp. strain GL1 liberates pyruvylated mannose from xanthan side chains

Article Abstract:

The bacterium Bacillus sp. strain GL1 was shown to have xanthan-depolymerizing enzymes when grown in a medium containing xanthan as the carbon source. The xanthan lyase purified from the culture fluid was a monomer with a molecular mass of 75 kDa and was most active at pH 5.5 and 50 degrees C. Results indicated that the enzyme cleaved the linkage between the terminal pyruvylated mannosyl and glucuronyl residues in the side chain of xanthan.

Polysaccharide lyase: molecular cloning, sequencing, and overexpression of the xanthan lyase gene of Bacillus sp. strain GL1

Article Abstract:

In Bacillus sp. strain GL1, xanthan lyase is processed in several steps. It is synthesized as a 99 kDa preproform, then converted to a 97 kDa precursor, and finally into the mature 75 kDa enzyme.

Microbial enzymes, Enzyme synthesis