Characterization of a novel lipase from Bacillus sp. isolated from tannery wastes.
Braz J Microbiol
; 42(1): 22-9, 2011 Jan.
Article
em En
| MEDLINE
| ID: mdl-24031600
ABSTRACT
Kinetics of a lipase isolated from Bacillus sp. was studied. The enzyme showed maximum activity at pH 9 and temperature 60°C. The Michaelis constant (KM 0.31 mM) obtained from three different plots i.e., Lineweaver-Burk, Hanes-Wolf and Hofstee, was found to be lower than already reported lipases that confirmed higher affinity of the enzyme for its substrate p-NPL (p-nitrophenyl laurate). Vmax of the enzyme was found to be 7.6 µM/mL/min. Energy of activation calculated from Arrhenius plot was found to be 20.607 kJmol(-1). Activation enthalpy (ΔH*) had negative trend and the value for the hydrolysis of p-NPL by the enzyme at optimum temperature was -2.748 kJmol(-1). Activation entropy (ΔS*) and free energy of activation (ΔG*) of the enzyme were found to be 1.468 Jmol(-1)K(-1) and -3.237 kJmol(-1), respectively at optimum temperature. Low value of Q10 (0.04788) shows high catalytic activity of the enzyme. Mn(2+), Fe(2+) and Mg(2+) enhanced the lipase activity whereas Cu(2+), Na(+) and Co(2+) inhibited the enzyme activity. However, the enzyme activity was not affected significantly by K(+) ions. EDTA and SDS also significantly inhibited the lipase activity. Activity of the enzyme was increased in n-hexane while decreased with increase in concentration of acetone, chloroform, ethanol and isopropanol.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Idioma:
En
Revista:
Braz J Microbiol
Ano de publicação:
2011
Tipo de documento:
Article
País de afiliação:
Paquistão