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Articles by Ponnuswamy Vijayaraghavan
Total Records ( 3 ) for Ponnuswamy Vijayaraghavan
  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.
  Ponnuswamy Vijayaraghavan , S.R. Flanet Raj and Samuel Gnana Prakash Vincent
  Fibrinolytic enzymes are agents that dissolve fibrin clots. These fibrinolytic agents have potential use to treat cardiovascular diseases, such as heart attack and stroke. The aim of the study was to purify fibrinolytic enzyme from the marine isolate, Pseudoalteromonas sp., IND11. Enzyme was purified to electrophoretic homogeneity using ammonium sulphate precipitation, ion exchange and affinity chromatography. The SDS-PAGE showed that it was a monomeric protein with an apparent molecular weight of 64 kDa. The purified enzyme was active at pH 6.0-9.0 with an optimum pH of 8.0. It was stable upto 50°C, exhibiting maximum activity between 30 and 60°C. Among the ions, Na+ and Ca2+ activated enzyme activity. The Fe2+ did not obviously activate or inhibit the enzyme activity. The ions such as Cu2+, Hg2+ and Zn2+ strongly affected enzyme activity. This enzyme activated plasminogen and also had direct clot lytic activity. It digested the fibrin net of blood clot, suggests its potential as an effective thrombolytic agent. This study explores new sources of fibrinolytic enzymes to treat and prevent CVDs.
  Ponnuswamy Vijayaraghavan , M. Kalaiyarasi and Samuel Gnana Prakash Vincent
  A low-cost culture medium for the production of bacterial alkaline protease was developed after response surface methodological approach. Central composite design was applied to optimize the concentration of the three significant factors, namely pH, sucrose and yeast extract. A second-order model equation was obtained and then validated experimentally. The model adequacy was highly satisfactory as the coefficient of determination was 0.98. The maximum enzyme production was 2213 U mL-1 after 72 h of incubation, which showed about fivefold increase in enzyme production than unoptimized medium. The partially purified enzyme showed optimum activity at 50°C at pH 9.0. Crude enzyme exhibited a significant stability with most of the tested commercial laundry detergents. This enzyme removed the gelatin layer of used X-ray film effectively. Considering its promising properties, Bacillus cereus IND6 enzymatic preparations may be considered a potential candidate for detergent applications and silver recovery.
 
 
 
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