Enzymatic synthesis of glyceride esters in solvent-free system: influence of the molar ratio, lipase source and functional activating agent of the support

• Autor(a) principal: Freitas,Larissa
• Data de Publicação: 2007
• Outros Autores: Perez,Victor H., Santos,Julio C., Castro,Heizir F. de
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Journal of the Brazilian Chemical Society (Online)
• Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532007000700011
• topic: glycerides; lipase; esterification; hybrid support; immobilization

This work assessed the influence of important factors that affect the synthesis of glyceride esters in solvent-free systems, such as: glycerol/fatty acid molar ratio, lipase source and activating agent of the support obtained by the sol-gel technique. Commercial lipase preparations were immobilized on polysiloxane-polyvinyl alcohol particles (POS-PVA) previously activated with different agents (glutaraldehyde, sodium metaperiodate and carbonyldiimidazole) and their performance on the esterification reaction was compared with commercial preparations of immobilized lipase (Lipozyme IM20, Novozym 435, Lipozyme RM IM and Lipozyme TL IM). The reaction medium containing excess glycerol favored the glyceride ester synthesis and the Lipozyme IM20 was found to be the most suitable immobilized lipase preparation, attaining molar conversions higher than 94%. The use of CAL B Lipase immobilized on POS-PVA also provided satisfactory performance (conversion of about 80%) and allowed the formation of 36% wt of 2,3-dihydroxypropyl dodecanoate (monolaurin).