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Characterization of a novel lipase from Bacillus sp. isolated from tannery wastes 58
Ghori,M. I; Iqbal,M. J; Hameed,A.
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...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Bacillus sp; Kinetic study; Lipases; P-Nitrophenyl laurate; Tannery wastes; Organic solvents.
Ano: 2011 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822011000100003
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