Functional characterization of a new holin-like antibacterial protein coding gene tmp1 from goat skin surface metagenome.

We have identified a holin-like gene from a goat skin surface metagenome. The ORF designated tmp1 coding for 34 amino acids shared sequence similarity with putative holin-like toxin genes. To analyze the antibacterial activity of tmp1 encoded protein, this ORF was cloned and expressed in Escherichia coli BL21(DE3).

Functional analysis of a putative holin-like peptide-coding gene in the genome of Bacillus licheniformis AnBa9.

BhlA, a putative holin-like protein of Bacillus licheniformis AnBa9 expressed in Escherichia coli BL21(DE3) showed antibacterial activity against several gram-positive bacteria including methicillin-resistant Staphylococcus aureus (MRSA) and Micrococcus luteus. Deletion analysis of bhlA suggests that a hydrophobic transmembrane domain, BhlATM is essential for antibacterial activity. Though the minimum inhibitory concentration (MIC) of BhlA was sevenfold lower than BhlATM, transmembrane domain deleted construct (BhlATM) had no antibacterial activity.

Influence of medium components and fermentation conditions on the production of bacteriocin(s) by Bacillus licheniformis AnBa9.

Recently, antibacterial peptides are gaining more attention as an alternative therapeutics and food and other products from spoilage and deterioration. Antibacterial peptide producing strains were isolated from sediments of slaughterhouse sewage wastes. One among them, identified as Bacillus licheniformis inhibited the growth of several gram positive bacteria.

Inhibition of proteases during fermentation improves xylanase production by alkali tolerant Aspergillus fumigatus ARl.

An alkali-tolerant Aspergillus fumigatus ARl produced a high level of xylanase (228 U/ml) at 42 h of submerged fermentation at pH 9.0. During later culture periods, xylanase activity declined considerably and reached 45 U/ml at 90 h.