Efficient transesterification of sucrose catalysed by the metalloprotease thermolysin in dimethylsulfoxide

N.R. Pedersen, P.J. Halling, L.H. Pedersen, R. Wimmer, R. Matthiesen, O.R. Veltman

Research output: Contribution to journalArticlepeer-review

36 Citations (Scopus)

Abstract

Thermolysin catalyses the formation of sucrose esters from sucrose and vinyl laurate in dimethylsulfoxide, with a specific activity of 53 nmol/min/mg and 2-O-lauroyl-sucrose as the main product. Such transesterification reactions are normally observed only when the mechanism involves an acyl enzyme intermediate, as with lipases or serine proteases, and not with metalloproteases like thermolysin. A possible reason is the affinity of the active site of thermolysin for sugar moieties, as for the potent inhibitor phosphoramidon. The reaction is not catalysed by other proteins under the same conditions, and is inhibited by removal of the active site zinc.
Original languageEnglish
Pages (from-to)181-184
Number of pages3
JournalFEBS Letters
Volume519
Issue number1-3
DOIs
Publication statusPublished - 22 May 2002

Keywords

  • transesterification
  • thermolysin
  • carbohydrate fatty acids ester
  • dimethylsulfoxide
  • reaction mechanism Enzymatic peptide-synthesis
  • regioselective esterification
  • lipase
  • acylation
  • protease
  • derivatives
  • alcohol

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