Abstract
Monomeric 30 kDa γ-glutamyl transpeptidase (GGT30) was purified from culture broth of Bacillus licheniformis ER-15 along with a heterodimeric 67 kDa GGT (GGT67). In presence of subtilisin, GGT30 had improved catalytic efficiency (Vmax/Km) of 59 min−1, altered pH and temperature optima of pH 11 and 70°C.and had salt-tolerant glutaminase activity. Glutaminase activity was retained even in protease-inhibited condition in presence of 2 mM PMSF. GGT30 and subtilisin complexation was also confirmed by relative electrophoretic mobility and fluorescence quenching experiment.
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Financial assistance from University of Delhi is duly acknowledged by the authors. Authors also thank Prof. Sheela Srivastava, Department of Genetics, University of Delhi for critically going through the manuscript.
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Tiwary, E., Gupta, R. Improved catalytic efficiency of a monomeric γ-glutamyl transpeptidase from Bacillus licheniformis in presence of subtilisin. Biotechnol Lett 32, 1137–1141 (2010). https://doi.org/10.1007/s10529-010-0271-3
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DOI: https://doi.org/10.1007/s10529-010-0271-3