Abstract: Lipases constitute one of the most important groups of
industrial enzymes that catalyze the hydrolysis of triacylglycerol to
glycerol and fatty acids. Muscarinic antagonist relieves smooth
muscle spasm of the gastrointestinal tract and effect on the
cardiovascular system. In this research the effect of a muscarinic
antagonist on the lipase activity of Pseudomonas aeruginosa was
studied. Lineweaver–Burk plot showed that the drug inhibited the
enzyme by competitive inhibition. The IC50 value (0.16 mM) and Ki
(0.03 mM) of the drug revealed the drug bound to enzyme with high
affinity. Determination of enzyme activity in various pH and
temperature showed that the maximum activity of lipase was at pH 8
and 60oC both in presence and absence of the drug.
Abstract: Immobilization of lipase enzyme produced from palm oil mill effluent (POME) by the activated carbon (AC) among the low cost support materials was optimized. The results indicated that immobilization of 94% was achieved by AC as the most suitable support material. A sequential optimization strategy based on a statistical experimental design, including one-factor-at-a-time (OFAT) method was used to determine the equilibrium time. Three components influencing lipase immobilization were optimized by the response surface methodology (RSM) based on the face-centered central composite design (FCCCD). On the statistical analysis of the results, the optimum enzyme concentration loading, agitation rate and carbon active dosage were found to be 30 U/ml, 300 rpm and 8 g/L respectively, with a maximum immobilization activity of 3732.9 U/g-AC after 2 hrs of immobilization. Analysis of variance (ANOVA) showed a high regression coefficient (R2) of 0.999, which indicated a satisfactory fit of the model with the experimental data. The parameters were statistically significant at p
Abstract: This paper studied the synthesis of monoacylglycerol (monolaurin) by glycerolysis of coconut oil and crude glycerol, catalyzed by Carica papaya lipase. Coconut oil obtained from cold pressed extraction method and crude glycerol obtained from the biodiesel plant in Department of Chemistry, Uttaradit Rajabhat University, Thailand which used oils were used as raw materials for biodiesel production through transesterification process catalyzed by sodium hydroxide. The influences of the following variables were studied: (i) type of organic solvent, (ii) molar ratio of substrate, (iii) reaction temperature, (iv) reaction time, (v) lipase dosage, and (vi) initial water activity of enzyme. High yields in monoacylglycerol (58.35%) were obtained with molar ratio of glycerol to oil at 8:1 in ethanol, temperature was controlled at 45oC for 36 hours, the amount of enzyme used was 20 wt% of oil and initial water activity of enzyme at 0.53.
Abstract: In this paper, naturally immobilized lipase, Carica
papaya lipase, catalyzed biodiesel production from fish oil was
studied. The refined fish oil, extracted from the discarded parts of
fish, was used as a starting material for biodiesel production. The
effects of molar ratio of oil: methanol, lipase dosage, initial water
activity of lipase, temperature and solvent were investigated. It was
found that Carica papaya lipase was suitable for methanolysis of fish
oil to produce methyl ester. The maximum yield of methyl ester
could reach up to 83% with the optimal reaction conditions: oil:
methanol molar ratio of 1: 4, 20% (based on oil) of lipase, initial
water activity of lipase at 0.23 and 20% (based on oil) of tert-butanol
at 40oC after 18 h of reaction time. There was negligible loss in
lipase activity even after repeated use for 30 cycles.
Abstract: Lipases are enzymes particularly amenable for
immobilization by entrapment methods, as they can work equally
well in aqueous or non-conventional media and long-time stability of
enzyme activity and enantioselectivity is needed to elaborate more
efficient bioprocesses. The improvement of Pseudomonas
fluorescens (Amano AK) lipase characteristics was investigated by
optimizing the immobilization procedure in hybrid organic-inorganic
matrices using ionic liquids as additives. Ionic liquids containing a
more hydrophobic alkyl group in the cationic moiety are beneficial
for the activity of immobilized lipase. Silanes with alkyl- or aryl
nonhydrolizable groups used as precursors in combination with
tetramethoxysilane could generate composites with higher
enantioselectivity compared to the native enzyme in acylation
reactions of secondary alcohols. The optimal effect on both activity
and enantioselectivity was achieved for the composite made from
octyltrimethoxysilane and tetramethoxysilane at 1:1 molar ratio (60%
increase of total activity following immobilization and enantiomeric
ratio of 30). Ionic liquids also demonstrated valuable properties as
reaction media for the studied reactions, comparable with the usual
organic solvent, hexane.