Data/hora: 16/06/2024 09:16:06

Provedor de dados: 	58	
País: 	Brazil	
Título: 	Characterization of a novel lipase from Bacillus sp. isolated from tannery wastes	
Autores: 	Ghori,M. I; Iqbal,M. J; Hameed,A.	
Data: 	2011-03-01	
Ano: 	2011	
Palavras-chave: 	Bacillus sp; Kinetic study; Lipases; P-Nitrophenyl laurate; Tannery wastes; Organic solvents.	
Resumo: 	Kinetics of a lipase isolated from Bacillus sp. was studied. The enzyme showed maximum activity at pH 9 and temperature 60ºC. The Michaelis constant (K M 0.31 µM) 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-1K-1 and -3.237 kJmol-1, respectively at optimum temperature. Low value of Q10 (0.04788) shows high catalytic activity of the enzyme. Mn2+, Fe2+ and Mg2+ enhanced the lipase activity whereas Cu2+, Na+ and Co2+ 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.	
Tipo: 	Info:eu-repo/semantics/article	
Idioma: 	Inglês	
Identificador: 	http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822011000100003	
Editor: 	Sociedade Brasileira de Microbiologia	
Relação: 	10.1590/S1517-83822011000100003	
Formato: 	text/html	
Fonte: 	Brazilian Journal of Microbiology  v.42 n.1 2011	
Fonte: 	info:eu-repo/semantics/openAccess