Purification and characterization of a keratinolytic serine proteinase from Streptomyces albidoflavus

Article Abstract:

Streptomyces strain K, which was identified as a strain of Streptomyces albidoflavus, secreted at least six extracellular proteases when it was cultured on feather meal-based medium. The major keratinolytic serine proteinase was purified to homogeneity by a two-step procedure. This enzyme had a molecular weight of 18,000 and was optimally active at acidity values ranging from 6 to 9.5 and at temperatures ranging from 40 to 70 degrees Celsius. Findings revealed that the enzyme was homologous to Streptomyces griseus protease B.

Proteases, Streptomyces, Serine, Keratin

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Biochemical and genetic characterization of enterocin A from Enterococcus faecium, a new antilisterial bacteriocin in the pediocin family of bacteriocins

Article Abstract:

Amino acid and DNA sequencings are performed to investigate the primary structure of enterocin A, a new antilisterial bacteriocin from Enterococcus faecium. Results show that the new bacteriocin belongs to the double-glycine leaders common in small nonlantibiotic bacteriocins. The measured data also suggest the presence of a second open reading frame which may encode the immunity factor of enterocin A.

Analysis, Antibiotics, DNA sequencers, Bacteriology, Antibiotic structure-activity relationships

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Biochemical and genetic characterization of coagulin, a new antilisterial bacteriocin in the pediocin family of bacteriocins, produced by Bacillus coagulans I(sub 4)

Article Abstract:

Researchers report the amino acid sequence of a pediocin-like peptide isolated from a non-lactic acid bacterium, Bacillus coagulans I(sub 4). It has 44 residues and only differs from the pediocins AcH and PA-1 by one amino acid at the C-terminus.

Reports, Bacterial toxins, Amino acid sequence, Amino acid sequencing

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