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Production of biodiesel fuel from triglycerides and alcohol using immobilized lipase

By: Publication details: 2001Description: 53-58Subject(s): Online resources: In: Journal of Molecular Catalysis B: Enzymatic 16Summary: TRANSCRIPCIÓN DEL RESUMEN PUBLICADO POR EL AUTOR: Transesterification reactionwas performed using triglycerides and short-chain alcohol by immobilized lipase in non-aqueous conditions. The long-chain fatty acid ester, which is the product of this reaction, can be used as a diesel fuel that does not produce sulfur oxide and minimize the soot particulate. Immobilized Pseudomonas fluorescens lipase showed the highest activity in this reaction. Immobilization of lipase was carried out using porous kaolinite particle as a carrier.When methanol and ethanol were used as alcohol, organic solvent like 1,4-dioxane was required. The reaction could be performed in absence of solvent when 1-propanol and 1-butanol were used as short-chain alcohol. The activity of immobilized lipase was highly increased in comparison with free lipase because its activity sites became more effective. Immobilized enzyme could be repeatedly used without troublesome method of separation and the decrease in its activity was not largely observed. © 2001 Elsevier Science
Item type: Artículo de Revista
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Artículoi publicado en el web site de THE UNIVERSITY OF AUCKLAND, Departmente of Chemical and Materials Engineering

TRANSCRIPCIÓN DEL RESUMEN PUBLICADO POR EL AUTOR: Transesterification reactionwas performed using triglycerides and short-chain alcohol by immobilized lipase in non-aqueous conditions. The long-chain fatty acid ester, which is the product of this reaction, can be used as a diesel fuel that does not produce sulfur oxide and minimize the soot particulate. Immobilized Pseudomonas fluorescens lipase showed the highest activity in this reaction. Immobilization of lipase was carried out using porous kaolinite particle as a carrier.When methanol and ethanol were used as alcohol, organic solvent like 1,4-dioxane was required. The reaction could be performed in absence of solvent when 1-propanol and 1-butanol were used as short-chain alcohol. The activity of immobilized lipase was highly increased in comparison with free lipase because its activity sites became more effective. Immobilized enzyme could be repeatedly used without troublesome method of separation and the decrease in its activity was not largely observed. © 2001 Elsevier Science



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