Synthesis of esters using a nylon-immobilized lipase in batch and continuous reactors.

Abstract:

:Direct esterifications using a nylon-immobilized lipase from Candida cylindracea were carried out in batch and continuous-flow reactors. The immobilized enzyme was effective in catalyzing the synthesis of ethylpropionate, isoamylpropionate, and isoamylbutyrate. With ethanol dissolved in hexane as a substrate, the maximum initial esterification rate was 0.02 mole/(h x g of immobilized protein), but the enzyme was stable only when the substrate concentrations were lower than 0.2 M. With isoamyl alcohol in hexane as a substrate, esterification rates as high as 0.085 mole/(h x g of immobilized protein) were observed and the immobilized enzyme was stable over a much broader concentration range. However, in this case, the use of a solvent, such as hexane, was not necessary for esterification, and the enzyme could be employed in equimolar acid/alcohol mixtures. A packed-bed reactor was operated successfully for the continuous synthesis of esters. The reactor was stable for long periods of time, and the steady-state performance could be accurately predicted on the basis of batch reaction experiments.

journal_name

Enzyme Microb Technol

authors

Carta G,Gainer JL,Gibson ME

doi

10.1016/0141-0229(92)90054-r

keywords:

subject

Has Abstract

pub_date

1992-11-01 00:00:00

pages

904-10

issue

11

eissn

0141-0229

issn

1879-0909

pii

0141-0229(92)90054-R

journal_volume

14

pub_type

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