Biochemical and phylogenetic analyses of a cold-active beta-galactosidase from the lactic acid bacterium Carnobacterium piscicola BA

Article Abstract:

Biochemical and phylogenetic analyses have been carried out for a cold-active beta-galactosidase from Carnobacterium piscicola BA, a lactic acid bacterium. The study was to give information that could be compared with that for higher-temperature counterparts. The enzyme studied is homologous to a thermophilic enzyme from Bacillus stearothermophilus. The purified enzyme was unstable and 10% glycerol was necessary to keep activity, the optimal temperature for which was 30 degrees C. At 40 degrees C it was inactivated in 10 min.

United States, Statistical Data Included, Usage, Enzymes, Bacteria, Thermophilic, Cold adaptation, Cladistic analysis, Molecular microbiology, Thermophiles

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Bioinformatic, genetic, and biochemical evidence that some glycoside hydrolase family 42 [beta]-galactosidases are arabinogalactan type I oligomer hydrolases

Article Abstract:

The genes neighboring glycoside hydrolase family (GHF) 42 genes in databases are analyzed to detect an arrangement implying that these enzymes might hydrolyze oligosaccharides released by GHF 53 enzymes from arabinogalactan type I, a pectic plant polysaccharide. In vivo evidence is provided for a function of some GHF 42 [beta]-galactosidases.

Science & research, Pennsylvania, Analysis, Genetic aspects, Bacillus subtilis, Thin layer chromatography, Glycosides

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Characterization of two new glycosyl hydrolases from the lactic acid bacterium Carnobacterium piscicola strain BA

Article Abstract:

Researchers have discovered two beta-galactosidases in Carnobacterium piscicola strain BA that may act synergistically with the alpha-galactosidase to degrade different polysaccharides. In particular, they found increased enzyme activity when cells supplemented with lactose were grown on a phosphorylated beta-galactoside substrate.

Microbial enzymes

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