Selectivity of Rhizomucor miehei lipase as affected by choice of cosubstrate system in ester modification reactions in organic media

Biotechnol Bioeng. 2000 Jul 20;69(2):222-6. doi: 10.1002/(sici)1097-0290(20000720)69:2<222::aid-bit11>3.0.co;2-8.

Abstract

Fatty acid (FA) selectivity of immobilized Rhizomucor miehei lipase was determined for various cosubstrate systems for ester modification involving competing n-acyl-donor substrates of even-chain length (C4-C16; FA or their methyl esters, FAME) and either n-propanol or propyl acetate in hexane. Acyl-chain-length optima were observed for C8 and C14/16 in all cases. Upon changing between cosubstrate systems of [FA + propanol] to [FAME + propanol] to [FAME + propyl acetate], there was a general shift in selectivity toward shorter-chain-length FA (C4-C8). The greatest degree of reaction selectivity (based on ratios of selectivity constants) among the FA substrates was 3.1 for the [FA + propanol], 2.5 for the [FAME + propanol], and 1.4 for the [FAME + propyl acetate] cosubstrate systems. For esterification reactions between C6 FA and reactive members of a series of aliphatic and aromatic alcohols, the greatest degree of selectivity observed was 3.6.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • 1-Propanol / metabolism
  • 2-Propanol / metabolism
  • Acetates / metabolism
  • Alcohols / metabolism
  • Biotechnology
  • Enzymes, Immobilized
  • Fatty Acids / chemistry
  • Fatty Acids / metabolism
  • Lipase / metabolism*
  • Rhizomucor / enzymology*
  • Substrate Specificity

Substances

  • Acetates
  • Alcohols
  • Enzymes, Immobilized
  • Fatty Acids
  • isopropyl acetate
  • propyl acetate
  • 1-Propanol
  • Lipase
  • 2-Propanol