Present investigation assessed the hypoglycemic potential of hydro-alcoholic (HAE) and aqueous (AQE) extracts of Mehon, a commercial antidiabetic polyherbal formulation using various in vitro techniques. HAE and AQE were analyzed for α-amylase and α-glucosidase inhibition, glucose adsorption, diffusion, and transport across yeast cells membrane. HAE showed higher αglucosidase (IC50:156.95 μg/ml) inhibition. Glucose adsorption increased with increment in glucose concentration (5mM/L-100mM/L). Rate of glucose uptake into yeast cells was linear. Both extracts exhibited time dependent glucose diffusion. Calculated GDRI was 27.44 %(HAE) and 17.43 %(AQE) at 30 min which reduced over time, thereby confirming the antihyperglycemic propensities of Mehon.
Alkaline protease production by a newly isolated Bacillus species from laundry soil was studied for detergent biocompatibility. From its morphological and nucleotide sequence (about 1.5 kb) of its 16S rDNA it was identifi ed as Bacillus species with similarity to Bacillus species Y (Gen Bank entry: ABO 55095), and close homology with Bacillus cohnii YN-2000 (Gen Bank entry: ABO23412). Partial purifi cation of the enzyme by ammonium sulfate (50-70% saturation) yielded 8-fold purity. Casein zymography and Sodium dodecylsulphate-Polyacrylamide gel electrophoresis (SDS-PAGE) of the partially purifi ed enzyme revealed two isozymes of molecular sizes approximately 66 kDa and 18 kDa, respectively. The enzyme was most active at pH 12 and 50°C. At pH 12 the enzyme was stable for 5 h and retained 60% activity. The enzyme retained 44% activity at 50°C up to 2 h. The protease showed good hydrolysis specifi city with different substrates tested. The presence of Mn 2+ , Co 2+ and ethylenediaminetetracetic acid (EDTA) showed profound increase in protease activity. The protease of Bacillus species Y showed excellent stability and compatibility with three locally available detergents (Kite, Tide and Aerial) up to 3 h retaining almost 70-80% activity and 10-20% activity at room temperature (30°C) and 50°C, respectively, indicating the potential role of this enzyme for detergent application.
The amine oxidase (AMO) plate assay screening procedure for isolation of the mutants deficient in inactivation of peroxisomal enzymes in the yeast Y. lipolytica has been developed. The first tagged mutants affected in the peroxisomal AMO and isocitrate lyase inactivation were generated by the insertion of a zeta-URA3 mutagenesis cassette into the genome of a zeta-free and игаЗ deletion mutant strain of Y. lipolytica.
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