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Bacillus brewis
Published in Yoshikatsu Murooka, Tadayuki Imanaka, Recombinant Microbes for Industrial and Agricultural Applications, 2020
Bacillus brevis generally shows only a weak proteinase activity in the culture medium, compared with B. subtilis. Especially, several strains, including HPD31, showed no detectable hydrolytic activity toward casein or bovine serum albumin [5]. In recent studies, we found a proteinaceous proteinase inhibitor secreted by 5. brevis HPD31 and 47 [7; unpublished observation]. Therefore, it is conceivable that a proteinase is produced by B. brevis, but is inactivated by the proteinase inhibitor. The various levels of proteinase activities among B. brevis strains might be due to the different levels of the proteinase inhibitor.
The purification and functional study of new compounds produced by Escherichia coli that influence the growth of sulfate reducing bacteria
Published in Egyptian Journal of Basic and Applied Sciences, 2020
Oluwafemi Adebayo Oyewole, Julian Mitchell, Sarah Thresh, Vitaly Zinkevich
Several studies have described some inhibitors of SRB growth that are derived from bacteria; for example, Jayaraman et al. [69] and Zuo [29] reported that indolicidin, bactenecin, and polymyxin produced by Paenibacillus polymyxa are capable of inhibiting SRB growth. Bacillus brevis produces a compound referred to as gramicidin-S that inhibits the growth of Desulfovibrio orientis, D. vulgaris and D. gigas [29,31,70] and thereby reduced corrosion caused by the SRB. In addition, Bacillus licheniformis secretes γ-polyglutamate and polyaspartate that reduce SRB growth [29,71,72]. The mechanism of SRB growth prevention by these organisms has been suggested and include either the production of antimicrobial agents [29,73] or attack on the adenosine 5ʹ- phosphosulphate (APS) and bisulfate reductase (DSR) responsible for hydrogen sulfide production in SRBs [14]. Similarly, the SGE may function in SRB induction by increasing their growth rate while the SGI may function by causing damage in the cells as observed in this study. The MALDI-TOF spectra showed the presence of low molecular weight compounds in the range of 1700 Da for SGE and 2400 Da for SGI. The spectra showed equal and repeating units of ~213 m/z between the peaks. According to Wallace and Guttman [74], the equal and repeating units are characteristic spectra of condensation homopolymers. MALDI-TOF spectra revealed that the compounds are small molecular weight biomolecules and that the two molecules are very closely related.
Isolation and characterization of a cold-active, alkaline, detergent stable α-amylase from a novel bacterium Bacillus subtilis N8
Published in Preparative Biochemistry and Biotechnology, 2018
The molecular weight of N8 α-amylase was almost 205 kDa and the zymography of the enzyme revealed a single amylolitic activity band on the gel containing starch (Figure 7). This result is similar to the extracellular α-amylase of Bacillus brevis MTCC 7521 (205 kDa),[10] and the amylase enzyme of Chloroflexus aurantiacus (210 kDa).[50]