Gas-phase enzymatic esterification on immobilized lipases in MCM-41 molecular sieves

Appl Biochem Biotechnol. 2002 Spring:98-100:963-76. doi: 10.1385/abab:98-100:1-9:963.

Abstract

Several lipolytic enzymes were immobilized in the pores of MCM-41 and Al-MCM-41 molecular sieves and used as catalysts in the gas-phase esterification of acetic acid with ethanol. The entrapment of enzymes depended on the molecular sieve and the type of enzyme used. The order of enzymatic activity for enzymes entrapped in the pores of MCM-41 and Al-MCM-41 in the esterification reaction was OF (Rhizopus niveus lipases) < FAP-15 (Rhizopus oryzae lipases) < LEX (Mucorjavanicus lipases) < PS (Pseudomonas cepacia lipases) < AK (Pseudomonas fluorescens lipases). Experiments carried out between 298 and 318 K showed no effect of temperature on catalyst yield, suggesting that the enzymes were appropriately immobilized in the pores of the molecular sieves, thus avoiding possible processes such as denaturing or autolysis.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Enzymes, Immobilized / metabolism*
  • Esters / metabolism
  • Ethanol / metabolism
  • Gases*
  • Indicators and Reagents
  • Kinetics
  • Lipase / metabolism*
  • Lipolysis / physiology*
  • Mucor / enzymology
  • Pseudomonas fluorescens / enzymology
  • Rhizopus / enzymology

Substances

  • Enzymes, Immobilized
  • Esters
  • Gases
  • Indicators and Reagents
  • Ethanol
  • Lipase