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Asian Journal of Biotechnology
  Year: 2011 | Volume: 3 | Issue: 5 | Page No.: 478-485
DOI: 10.3923/ajbkr.2011.478.485
 
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Purification and Properties of Novel Malate Dehydrogenase Isolated from Pseudomonas aeruginosa
Ponnuswamy Vijayaraghavan, Surgen A. Bright, Anuj Nishanth Lipton and S.G. Prakash Vincent

Abstract:
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.
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How to cite this article:

Ponnuswamy Vijayaraghavan, Surgen A. Bright, Anuj Nishanth Lipton and S.G. Prakash Vincent, 2011. Purification and Properties of Novel Malate Dehydrogenase Isolated from Pseudomonas aeruginosa. Asian Journal of Biotechnology, 3: 478-485.

DOI: 10.3923/ajbkr.2011.478.485

URL: https://scialert.net/abstract/?doi=ajbkr.2011.478.485

 
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