Purification and Properties of Novel Malate Dehydrogenase Isolated from Pseudomonas aeruginosa


	Asian Journal of Biotechnology
	Year: 2011 \| Volume: 3 \| Issue: 5 \| Page No.: 478-485 DOI: 10.3923/ajbkr.2011.478.485

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 k_m 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.

PDF Fulltext XML References Citation Report Citation

RELATED ARTICLES:

•	Characterization of a Novel Surfactant and Organic Solvent Stable High-alkaline Protease from New Bacillus pseudofirmus SVB1

•	Alteration of the Profile of Organic Acid Content and Exudation under Aluminum Stress in Maize (Zea mays L.)

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

COMMENT ON THIS PAPER

Navigation


		Online First
		Current Issue
		Previous Issues
		Editorial Board
		Submit a Manuscript
		Guide to Authors
		Subscribe to E-alerts

Indexed In


		ASCI-Database
		Asian Digital Library
		Cambridge Scientific Abstract
		Chemical Abstract Services
		Google Scholar

Follow @scialert

Science Alert