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Purification and characterization of a novel thermo-active amidase from Geobacillus subterraneus RL-2a

Content Provider	Springer Nature Link
Author	Mehta, Praveen Kumar Bhatia, Shashi Kant Bhatia, Ravi Kant Bhalla, Tek Chand
Copyright Year	2013
Abstract	A thermostable amidase produced by Geobacillus subterraneus RL-2a was purified to homogeneity, with a yield of 9.54 % and a specific activity of 48.66 U mg−1. The molecular weight of the native enzyme was estimated to be 111 kDa. The amidase of G. subterraneus RL-2a is constitutive in nature, active at a broad range of pH (4.5–11.5) and temperature (40–90 °C) and has a half-life of 5 h and 54 min at 70 °C. Inhibition of enzyme activity was observed in the presence of metal ions, such as Co2+, Hg2+, Cu2+, Ni2+, and thiol reagents. The presence of mid-chain aliphatic and amino acid amides enhances the enzymatic activity. The acyl transferase activity was detected with propionamide, butyramide and nicotinamide. The enzyme showed moderate stability toward toluene, carbon tetrachloride, benzene, ethylene glycol except acetone, ethanol, butanol, propanol and dimethyl sulfoxide. The K m and V max of the purified amidase with nicotinamide were 6.02 ± 0.56 mM and 132.6 ± 4.4 μmol min−1 mg−1 protein by analyzing Michaelis–Menten kinetics. The results of MALDI-TOF analysis indicated that this amidase has homology with the amidase of Geobacillus sp. C56-T3 (gi\|297530427). It is the first reported wide-spectrum thermostable amidase from a thermophilic G. subterraneus.
Starting Page	637
Ending Page	648
Page Count	12
File Format	PDF
ISSN	14310651
Journal	Extremophiles
Volume Number	17
Issue Number	4
e-ISSN	14334909
Language	English
Publisher	Springer Japan
Publisher Date	2013-05-26
Publisher Place	Japan
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	(Extreme) thermophilic microorganisms and their enzymology Biochemical characterization Enzyme stability Industrial enzymes Microbiology Biotechnology Biochemistry Microbial Ecology
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Medicine Microbiology

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