Stability of immobilized Rhizomucor miehei lipase for the synthesis of pentyl octanoate in a continuous packed bed bioreactor

Brazilian Journal of Chemical Engineering. 2014;31(3):633-641 DOI 10.1590/0104-6632.20140313s00002978

 

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Journal Title: Brazilian Journal of Chemical Engineering

ISSN: 0104-6632 (Print); 1678-4383 (Online)

Publisher: Brazilian Society of Chemical Engineering

LCC Subject Category: Technology: Chemical technology: Chemical engineering

Country of publisher: Brazil

Language of fulltext: English

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AUTHORS

E. Skoronski (Universidade do Estado de Santa Catarina)
N. Padoin (Universidade Federal de Santa Catarina)
C. Soares (Universidade Federal de Santa Catarina)
A. Furigo Jr. (Universidade Federal de Santa Catarina)

EDITORIAL INFORMATION

Peer review

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Time From Submission to Publication: 12 weeks

 

Abstract | Full Text

The enzymatic synthesis of organic compounds in continuous bioreactors is an efficient way to obtain industrially important chemicals. However, few works have focused on the study of the operational conditions and the bioprocess performance. In this work, the aliphatic ester pentyl octanoate was obtained by direct esterification using a continuous packed bed bioreactor containing the immobilized enzyme Lipozyme® RM IM as catalyst. Enzymatic deactivation was evaluated under different conditions for the operational parameters substrate/enzyme ratio (5.00, 1.67, 0.83 and 0.55 mmol substrate∙min-1∙g-1enzyme) and temperature (30, 40, 50 and 60 °C). The optimal condition was observed at 30 ºC, which gave the minimum enzymatic deactivation rate and the maximum conversion to the desired product, yielding approximately 60 mmols of ester for an enzyme loading of 0.5 g into the bioreactor. A first-order deactivation model showed good agreement with the experimental data.