Search results for: P. Pinyaphong

Authors: P. Pinyaphong, P. Sriburi, S. Phutrakul

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.

Keywords: biodiesel fuel production, methanolysis, fish oil, Carica papaya lipase.

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Authors: P. Pinyaphong, P. Sriburi, S. Phutrakul

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.

Keywords: Monoacylglycerol, crude glycerol, coconut oil, Carica papaya lipase.

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Authors: P. Pinyaphong, S. Phutrakul

Abstract:

Palm oil could be converted to cocoa butter equivalent by lipase-catalyzed interesterification. The objective of this research was to investigate the structure modification of palm oil to cocoa butter equivalent using Carica papaya lipase –catalyzed interesterification. The study showed that the compositions of cocoa butter equivalent were affected by acyl donor sources, substrate ratio, initial water of enzyme, reaction time, reaction temperature and the amount of enzyme. Among three acyl donors tested (methyl stearate, ethyl stearate and stearic acid), methyl stearate appeared to be the best acyl donor for incorporation to palm oil structure. The best reaction conditions for cocoa butter equivalent production were : substrate ratio (palm oil : methyl stearate, mol/mol) at 1 : 4, water activity of enzyme at 0.11, reaction time at 4 h, reaction temperature at 45 ° C and 18% by weight of the enzyme. The chemical and physical properties of cocoa butter equivalent were 9.75 ± 0.41% free fatty acid, 44.89 ± 0.84 iodine number, 193.19 ± 0.78 sponification value and melting point at 37-39 °C.

Keywords: Carica papaya lipase, cocoa butter equivalent, interesterification, palm oil.

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