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1.
Bioresour Technol ; 101(23): 8948-54, 2010 Dec.
Article in English | MEDLINE | ID: mdl-20675129

ABSTRACT

The objective of this research is to investigate the potential of transesterification of crude palm oil (CPO) to biodiesel at 30 degrees C. The mass transfer limitations problem crucial at 30 degrees C due to the viscosity of CPO has been addressed. The process parameters that are closely related to mass transfer effects like enzyme loading, agitation speed and reaction time were optimized. An optimum methanol to oil substrate molar ratio at 6.5:1 was observed and maintained throughout the experiments. The optimum operating condition for the transesterification process was found at 6.67 wt% of enzyme loading and at 150 rpm of agitation speed. The corresponding initial reaction and FAME yield obtained at 6 h were 89.29% FAME yield/hr and 85.01%, respectively. The 85% FAME yield obtained at 30 degrees C operation of CPO transesterification shows that the process is potentially feasible for the biodiesel synthesis.


Subject(s)
Biotechnology/methods , Plant Oils/metabolism , Temperature , Analysis of Variance , Esterification , Esters/analysis , Feasibility Studies , Kinetics , Lipase/metabolism , Models, Chemical , Palm Oil
2.
Bioresour Technol ; 101(16): 6558-61, 2010 Aug.
Article in English | MEDLINE | ID: mdl-20363621

ABSTRACT

In order to characterize enzyme activity and stability corresponding to temperature effects, thermodynamic studies on commercial immobilized lipase have been carried out via enzymatic transesterification. An optimum temperature of 40 degrees C was obtained in the reaction. The decreasing reaction rates beyond the optimum temperature indicated the occurrence of reversible enzyme deactivation. Thermodynamic studies on lipase denaturation exhibited a first-order kinetics pattern, with considerable stability through time shown by the lipase as well. The activation and deactivation energies were 22.15 kJ mol(-1) and 45.18 kJ mol(-1), respectively, implying more energy was required for the irreversible denaturation of the enzyme to occur. At water content of 0.42%, the initial reaction rate and FAME yield displayed optimum values of 3.317 g/L min and 98%, respectively.


Subject(s)
Biofuels , Enzymes, Immobilized/metabolism , Lipase/metabolism , Thermodynamics , Biocatalysis , Chromatography, Gas , Esterification , Kinetics , Lipase/antagonists & inhibitors , Temperature
3.
Bioresour Technol ; 99(8): 2724-35, 2008 May.
Article in English | MEDLINE | ID: mdl-17697778

ABSTRACT

Efforts in optimizing reducing agents, cysteine-HCl.H2O and sodium sulfide in order to attain satisfactory responses during acetic acid fermentation have been carried out in this study. Cysteine-HCl.H2O each with five concentrations (0.00-0.50 g/L) was optimized one at a time and followed by sodium sulfide component (0.00-0.50 g/L). Response surface methodology (RSM) was used to determine the optimum concentrations of cysteine-HCl.H2O and sodium sulfide. The statistical analysis showed that the amount of cells produced and efficiency in CO conversion were not affected by sodium sulfide concentration. However, sodium sulfide is required as it does influence the acetic acid production. The optimum reducing agents for acetic acid fermentation was at 0.30 g/L cysteine-HCl.H2O and sodium sulfide respectively and when operated for 60 h cultivation time resulted in 1.28 g/L acetic acid production and 100% CO conversion.


Subject(s)
Acetic Acid/metabolism , Clostridium/metabolism , Biometry , Clostridium/drug effects , Cysteine/pharmacology , Fermentation , Freeze Drying , Gases/metabolism , Kinetics , Sulfides/pharmacology
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