Comparison of two-phase lipase-catalyzed esterification on micro and bench scale

J.W. Swarts, P. Vossenberg, M.H. Meerman, A.E.M. Janssen, R.M. Boom

Research output: Contribution to journalArticleAcademicpeer-review

35 Citations (Scopus)

Abstract

Lipase type B from Candida antarctica was used to catalyze the esterification of propionic acid and 1-butanol in a water/n-decane two-phase system on micro and on bench scale. The reaction was described by a Ping Pong Bi Bi mechanism with alcohol inhibition. The kinetic parameters on micro and bench scale were compared; no significant differences were found. Furthermore, effects of temperature on activation and inactivation of the enzyme were found to be similar on micro and bench scale. Therefore, parameters found on either scale can be used for the other scale. Enzyme kinetic parameters can be determined on a micro scale, with very low consumption of reagents and catalyst, and then be applied to bench scale. This can reduce the cost of optimizing enzyme processes by downscaling
Original languageEnglish
Pages (from-to)855-861
JournalBiotechnology and Bioengineering
Volume99
Issue number4
DOIs
Publication statusPublished - 2008

Keywords

  • immobilized lipase
  • parameters
  • kinetics
  • hexane

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