Cyanobacteria from habitats within Gujarat have been poorly studied with regard to their diversity. In the present investigation eight morphologically distinct cyanobacterial isolates were obtained and characterized from the fresh water and marine habitats. Identification was performed based on morphological features and on 16S rDNA sequences analysis. A phylogenetic tree based on 16S rDNA sequence of cyanobacterial isolates was prepared. Phylogenetic analysis clustered the eight morphologically distinct isolates into two distinct groups thus highlighting the importance of both morphological and genetic methods in studying cyanobacterial diversity.
Solid state fermentation of wheat straw was attempted with P. chrysosporium MTCC 787 for production of MnP at 39ºC. Fermented residue was extracted with 0.2 M sodium tartarate buffer (pH 3) and was subjected to ammonium sulfate precipitation. Precipitates obtained were subjected to MnP assay, upon dialysis, using MBTH and DMAB as substrate. Optimum pH and temperature were reported to be pH 4.5 and 30ºC respectively. Km and Vmax of MnP for MBTH were found to be 0.05 mM and 25 U/mg, respectively. Enzyme kinetics were also assessed against Reactive Black B (RBB), a widely used textile diazo dye, as substrate. Km and Vmax of MnP for RBB were reported as 0.2 mM and 7 U/mg, respectively. These findings suggest enormous potential of MnP of P. chrysosporium MTCC 787 for its application in treatment of RBB containing wastewater.
Thermophilic lipases are stable at higher temperatures, which enhance their demand in industrial applications. In the present study, thermostable lipase was produced from bacterial strain Bacillus subtilis SHVSC04 (MN565992) isolated from Tuva Timba hot spring, Gujarat, India. Isolate displayed maximum growth in basal medium augmented with 3% sucrose, 3% yeast extract and 2 % salt at pH 7 and 50°C in 48 h. Whereas, isolate produced maximum lipase in tributyrin agar medium with pH 7, enriched with 3% sucrose, 3% yeast extract and incubated at 50°C in 72 h. Tributyrin (2%) was found to be the best substrate for lipase production in submerged conditions. The amount of lipase was increased by 1.5 fold upon optimization of different environmental and nutritional parameters. The enzyme retained 84% activity at 60°C and 70% of activity at 70°C for 1h. The present findings advocate that hot springs in Gujarat are a substantial source of thermostable bacteria producing enzymes of industrial importance.
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