Literature DB >> 19943181

Transesterification of oil mixtures catalyzed by microencapsulated cutinase in reversed micelles.

Sara M Badenes1, Francisco Lemos, Joaquim M S Cabral.   

Abstract

Recombinant cutinase from Fusarium solani pisi was used to catalyze the transesterification reaction between a mixture of triglycerides (oils) and methanol in reversed micelles of bis(2-ethylhexyl) sodium sulfosuccinate (AOT) in isooctane for the purposes of producing biodiesel. The use of a bi-phase lipase-catalyzed system brings advantages in terms of catalyst re-use and the control of water activity in the medium and around the enzyme micro-environment. Small-scale batch studies were performed to study the influence of the initial enzyme and alcohol concentrations, and the substrates molar ratio. Conversions in excess of 75 were obtained with reaction times under 24 h, which makes this enzymatic process highly competitive when compared to similar lipase catalyzed reactions for biodiesel production using methanol.

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Year:  2009        PMID: 19943181     DOI: 10.1007/s10529-009-0172-5

Source DB:  PubMed          Journal:  Biotechnol Lett        ISSN: 0141-5492            Impact factor:   2.461


  1 in total

1.  Influence of surface charge, binding site residues and glycosylation on Thielavia terrestris cutinase biochemical characteristics.

Authors:  Abhijit N Shirke; Danielle Basore; Samantha Holton; An Su; Evan Baugh; Glenn L Butterfoss; George Makhatadze; Christopher Bystroff; Richard A Gross
Journal:  Appl Microbiol Biotechnol       Date:  2016-01-13       Impact factor: 4.813

  1 in total

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