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Articles by S.G. Prakash Vincent
Total Records ( 2 ) for S.G. Prakash Vincent
  Ponnuswamy Vijayaraghavan , Surgen A. Bright , Anuj Nishanth Lipton and S.G. Prakash Vincent
  The aim of this study was to purify and characterize citric acid cycle enzyme malate dehydrogenase (MDH; EC 1. 1. 1. 37) from Pseudomonas aeruginosa. The purification steps consisted of ammonium sulphate precipitation, ion-exchange chromatography and gel filtration. A typical procedure provided 638-fold purification with 23.0% yield. Single band was observed in both native gradient-and SDS-PAGE. The molecular weight estimated for the native enzyme was 70.5 kDa whereas subunit values of 36 kDa were determined. Hence, MDH is a dimer of identical subunits. The enzyme was highly active at pH 8.0 when NADH was used as the cofactor and was highly stable at pH 7.0. The optimum temperature for the enzyme activity was recorded to be 40°C. Oxaloacetate was determined as the specific substrate with an apparent km of 10 μM. The characteristics of thermo-stability and its high activity at alkaline pH suggest its potential diagnostic, therapeutic and beverage related applications. This MDH may be of value in developing a serological test for pneumonia which is caused by P. aeruginosa.
  P. Vijayaraghavan , C.S. Remya and S.G. Prakash Vincent
  α-Amylase is an important enzyme used in the industry and accounts for approximately 30% of the enzyme market. In the present study, Solid-State Fermentation (SSF) was carried out using banana peel, cabbage leaf, tapioca peel and wheat bran as substrates for α-amylase production by a fungus, Rhizopus microsporus. Among the four substrates used, the tapioca peel was found to yield the maximum (79 U g-1) and wheat bran supported 64 U g-1 of amylase production. The present study proved that the tapioca peel was a superior medium for the production of α-amylase than wheat bran for R. microsporus. The maximum production of α-amylase was recorded after 96 h of fermentation, initial pH = 6.0 and moisture content 60% (v/w). Enzyme production was high in the solid substrate (tapioca peel) containing 30% fungal inoculum (v/w), 1% xylose and 1% urea. Enzyme activity was found to be high at the pH 6.0 and the temperature at 40°C with 2% starch (m/v) and 10 mM of calcium ion concentration. This enzyme was fractionated with solid ammonium sulphate and partially purified by sephadex G 75 gel filtration chromatography. The amylase activity was determined by native polyacrylamide gel electrophoresis. Results of the present study indicate that the tapioca peel is the potential medium for the production of α-amylase by R. microsporus. This study also suggests the use of banana peel and cabbage leaf for the production of α-amylase.
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