Research Article

Purification and Properties of Glutamate-phenylpyruvate Aminotransferase from Rumen Bacterium Prevotella albensis

Md. Ruhul Amin, Ryoji Onodera, R. Islam Khan, R. John Wallace and C. Jamie Newbold

Glutamate-phenylpyruvate aminotransferase (GPAase) from a cell free extract of a rumen bacterium Prevotella albensis was purified 36-folds. The molecular weight of the GPAase was estimated to be 39.0 kDa by SDS-PAGE. The optimum pH of GPAase was 6.2 and the activity declined markedly above pH 8.5. GPAase was reactive over a wide range from pH 4.5 to 10.5. The maximum reaction velocity of GPAase was observed at a temperature of 50°C and at higher temperatures over 60°C, the activity declined. The GPAase was stable below 60°C. Most of the chemical agents and metal ions showed inhibition effects on GPAase activity.

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Md. Ruhul Amin, Ryoji Onodera, R. Islam Khan, R. John Wallace and C. Jamie Newbold, 2001. Purification and Properties of Glutamate-phenylpyruvate Aminotransferase from Rumen Bacterium Prevotella albensis. Pakistan Journal of Biological Sciences, 4: 1377-1381.

DOI: 10.3923/pjbs.2001.1377.1381

URL: https://scialert.net/abstract/?doi=pjbs.2001.1377.1381

Pakistan Journal of Biological Sciences

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Authors

Md. Ruhul Amin

Ryoji Onodera

R. Islam Khan

R. John Wallace

C. Jamie Newbold

Keywords

Research Article

Purification and Properties of Glutamate-phenylpyruvate Aminotransferase from Rumen Bacterium Prevotella albensis

How to cite this article

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