Research Journal of Engineering and Technology

J. Niranjan ¹, Fazal Basha ¹, G. Suganya ¹, M. Anil Kumar ¹, M. Seenuvasan ¹, S. Selvanaveen ¹

Affiliations
1 Department of Biotechnology, Madha Engineering College, Chennai, IN

Abstract

The industrially used biopolymer levan as an emulsifying agent was produced in large amounts by optimizing the physical parameters like pH, temperature and incubation time, with the central composite design under the response surface methodology where the maximum yield of levan was found to be 268 μg/ml at a pH of 8.0, a temperature of 20°C and the incubation period of 24^th h. The pH- and thermal stabilities of levan-forming activity were studied and arrived at the maximum activity at pH 7.0 and at 20°C respectively, thereby inferring that the levan is optimally produced by Bacillus subtilis in an alkaline environment. Scanning electron microscope was used to examine the surface morphology levan-producing Bacillus subtilis that showed the levan polymer as white dust-like particles.

Keywords

Bacillus subtilis, Levan Polymer, RSM, Scanning Electron Microscope.

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T. Uma ¹, V. N. Saranya ¹, M. Anil Kumar ¹, S. Selvanaveen ¹, R. Viveka ¹, M. Seenuvasan ¹

Affiliations
1 Department of Biotechnology, Madha Engineering College, Chennai, IN

Abstract

The extra cellular lipase produced by a novel strain of Bacillus sp. isolated from soil was used as an alternative for commercially available detergents for removing stains like oil, grease and blood stains in fabric clothes, as lipase shows the effect of hydrolysis of fat. The production was carried out by submerged fermentation using olive oil as substrate. The production media was optimized using the Response Surface Methodology (RSM) to get maximum yield with at most lipase activity. Thus Lipase produced had highest activity at pH 8, 30°C under incubation period of 24 h. The dialyzed sample of the partially purified enzyme was used to determine the molecular weight of lipase using sodium do-decyl sulphate poly acryl amide gel electrophoresis, which was 95 kDa. The stability of the enzyme was studied inferring it with maximum activity at pH 8.0 and temperature of 30°C. The detergent action of the enzyme was analyzed using the ultra filtered enzyme samples. The stain removal capacity of the lipase was better than the commercial detergents used.

Keywords

Bacillus sp., Lipase, Activity, pH, Temperature, RSM.

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M. B. Nishita ¹, Remya Rachel Chacko ¹, M. Anil Kumar ¹, D. Suresh ¹, S. Selvanaveen ¹, M. Seenuvasan ¹

Affiliations
1 Department of Biotechnology, Madha Engineering College, Chennai 600 069, IN

Abstract

A novel fibrinolytic enzyme from two different blood fibrin Bos taurus and Ovis aries as an added ingredient by Rhizomucor sp. which was purified by ammonium sulphate precipitation, dialysis and ion exchange chromatography. The purification protocol resulted in 1.373 and 1.737 -fold purification of the enzyme. The apparent molecular weight of the enzyme was found to be 30.0kDa, determined by sodium dodecylsulphate poly acrylamide gel electrophoresis. Optimal temperature and pH of the nattokinase were to be at 37°C and 8.0 respectively. Upon the addition of zinc chloride the enzyme activity was increased while EDTA and PMSF inhibited the activity of the enzyme, indicating the presence of metalloproteases. The produced enzyme showcases the blood clot-busting activity.

Keywords

Nattokinase, Bos taurus, Ovis aries, Rhizomucor sp.

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