Isolation and characterization of a polynucleotide phosphorylase from Bacillus amyloliquefaciens.

Production and biochemical characterization of a thermostable phytase from Bacillus amyloliquefaciens LOR10

Phytase can improve the nutritional value of plant-based foods by enhancing protein digestibility and mineral availability through phytate digestion in the stomach and the food processing industry. Microbial sources are more promising for the production of phytases on a commercial scale. The objectives of this exploration were to screening and isolation of phytase-producing bacteria from hot sp...

Isolation, Identification, and Characterization of a Cellulolytic Bacillus amyloliquefaciens Strain SS35 from Rhinoceros Dung

Cellulose hydrolyzing bacteria were isolated from rhinoceros dung and tested for clear zone formation around the colonies on the agar plates containing the medium amended with carboxymethylcellulose as a sole carbon source. Isolates were further screened on the basis of carboxymethylcellulase production in liquid medium. Out of 36 isolates, isolate no. 35 exhibited maximum enzyme activity of 0....

Isolation and characterization of a DNA probe for Staphylococcus aureus subspecies aureus biovar.

The gene encoding for polynucleotide phosphorylase (pnp) of a new biovar of Staphylococcus aureus subsp. aureus (NBSA) has been isolated from a genomic library of strain M280(0). The coding region consisted of a 1094-bp HindIII-HindIII DNA fragment encoding for a protein of 277 amino acids with a calculated molecular mass of 29.5 kDa. The nucleotide sequence of the structural gene, contained a ...

Thermostable α-amylase from Lignocellulosic Residues Using Bacillus amyloliquefaciens

tetA(L) mutants of a tetracycline-sensitive strain of Bacillus subtilis with the polynucleotide phosphorylase gene deleted.

A Bacillus subtilis strain with the polynucleotide phosphorylase gene deleted was sensitive for growth in the presence of tetracycline. This strain was used to select for tetracycline-resistant mutants. A point mutation in the tetA(L) promoter and a spontaneously occurring tetA(L) gene copy number mutant were characterized.