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Development of a catalytically stable and efficient lipase through an increase in hydrophobicity of the oxyanion residue

Abdul Wahab, Roswanira and Basri, Mahiran and Raja Abdul Rahman, Raja Noor Zaliha and Salleh, Abu Bakar and Abdul Rahman, Mohd. Basyaruddin and Leow, Thean Chor (2015) Development of a catalytically stable and efficient lipase through an increase in hydrophobicity of the oxyanion residue. Journal Of Molecular Catalysis B: Enzymatic, 122 . pp. 282-288. ISSN 1381-1177

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Abstract

In-silico and empirical site-directed substitutions of oxyanion Q114 of the wildtype T1 lipase with that of hydrophobic Leu and Met residues were carried out to afford the Q114L and Q114M lipases, respectively. Using the esterification production of menthyl butyrate as a reaction model, evaluation on the catalytic efficiency of the three lipases was performed. It was found that Leu evidently improved the catalytic activity of the Q114L lipase, achieving the highest conversions of menthyl butyrate under varying experimental conditions that may be attributable to its lower total energy when compared with both the T1 and Q114M lipases. The diminishing catalytic activity of T1 lipase observable following substitution with Met (Q114M lipase) may be due to formation of three additional cavities within the vicinity of the mutation, lesser density of the protein core and susceptibility to high temperature, particularly under prolonged reaction time. Therefore, it can be concluded that the substitution of Leu into the oxyanion-114 had rendered favorable structural changes that enhanced the catalytic activity of the T1 lipase, envisaging that such approach may also be of applied value for improving the catalytic activity of other bacterial lipases within the I.5 family.

Item Type:Article
Uncontrolled Keywords:geobacillus, in-silico, lipase, oxyanion, site-directed mutagenesis
Subjects:A General Works
ID Code:58281
Deposited By: Haliza Zainal
Deposited On:04 Dec 2016 12:07
Last Modified:15 Feb 2017 09:43

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