Genomic Organization of Streptomyces flavotricini NGL1 and Streptomyces erythrochromogenes HMS4 Reveals Differential Plant Beneficial Attributes and Laccase Production Capabilities.

The genus Streptomyces has been explored in industrial sectors due to its endurance to environmental stresses, the production of a plethora of biomolecules, the biological remediation of soils, and alleviating plant stresses. The whole genome of NGL1 and HMS4 was sequenced due to the specific laccase activity against 2,6-dimethoxyphenol (2,6-DMP) and differential plant beneficial attributes. The deduced genome of 8.85 Mbp and 7.73 Mbp in size with a G+C content of 72.03% and 72.3% was obtained for NGL1 and HMS4, respectively. A total of 8438 and 7322 protein coding genes, 155 (130 tRNA, 25 rRNA) and 145 tRNA (121 tRNA, 24 rRNA) coding genes were predicted in NGL1 and HMS4, respectively. The comparative genomics of NGL1 and HMS4 showed 185 and 162 genes encoding for carbohydrate-active enzymes, respectively. The genomic ability of these strains to encode carbohydrate-active enzymes, laccase, and diversity of BGCs, along with plant beneficial attributes to suppress the plant pathogens can be used for several industrial and agricultural applications.

Streptomyces: host for refactoring of diverse bioactive secondary metabolites.

Microbial secondary metabolites are intensively explored due to their demands in pharmaceutical, agricultural and food industries. Streptomyces are one of the largest sources of secondary metabolites having diverse applications. In particular, the abundance of secondary metabolites encoding biosynthetic gene clusters and presence of wobble position in Streptomyces strains make it potential candidate as a native or heterologous host for secondary metabolite production including several cryptic gene clusters expression. Here, we have discussed the developments in Streptomyces strains genome mining, its exploration as a suitable host and application of synthetic biology for refactoring genetic systems for developing chassis for enhanced as well as novel secondary metabolites with reduced genome and cleaned background.

Purification and characterization of a novel white highly thermo stable laccase from a novel Bacillus sp. MSK-01 having potential to be used as anticancer agent.

Laccases are multicoopper oxidases catalyzing the oxidation of phenolic as well as non-phenolic compounds. Laccases show typical blue color due to the presence of covalent Type 1 Cu-Cys bond which absorbs at 600 nm. However, recently some white laccases have also been identified which lacks typical spectra of blue laccases and do not show peak at 600 nm. In the present study, a novel white laccase was isolated from Bacillus sp. MSK-01. MSK laccase was purified and characterized in detail and the purified laccase was referred to MSKLAC. It has a molecular weight of 32 KDa. UV-visible spectrum of purified MSKLAC do not show characteristic peak at 600 nm and bend at 330 nm. The enzyme was repressed by conventional inhibitors of laccase like sodium azide, cysteine, dithiothreitol and ß-mercaptoethanol. The laccase was highly thermo-stable enzyme having optimum temperature of 75 °C and could treasure more than 50% activity even at 100 °C. The optimum pH for ABTS and guaiacol was 4.5 and 8.0 respectively. MSKLAC was stable in the presence of most of the metal ions and surfactants. The effect of MSKLAC on lung cancer cell line was also assessed. It was observed that MSKLAC is inhibitory to lung cell cancer line. Thus, MSKLAC has potential to be used as an anti-proliferative agent to cancer cells.

Immobilization of laccase-ABTS system for the development of a continuous flow packed bed bioreactor for decolorization of textile effluent.

Decolourization of textile effluent is always being a problem of major concern for the safe disposal of effluent water in river stream. Due to intense colour of the effluent water, even after the treatment, disposal of the water in river stream is under strict environmental regulation. Laccase, a natural oxidase, have the miraculous power to decolourize different dyes with or without mediators. However, stability and cost of implementation of the enzyme at industrial conditions make the entire process unfeasible at industrial scale. In the present study, a highly thermo-alkali-stable, metal, surfactant and organic solvent tolerant laccase from Bacillus sp. MSK-01 was immobilized in Cu-alginate bead with ABTS mediator under standardized conditions. A continuous flow packed bed bioreactor was formulated to develop a continuous method of the treatment of effluent water. Results showed 66% reduction in the colour of the effluent. UV-VIS spectrum analysis of the treated and untreated samples showed the formation of the degradation products of dyes due to the action of laccase. The developed process can be made useful for on site industrial application.