Mycobacterium smegmatis acyltransferase: The big new player in biocatalysis

Biotechnol Adv. 2022 Oct:59:107985. doi: 10.1016/j.biotechadv.2022.107985. Epub 2022 May 21.

Abstract

After several decades during which proteases and after lipases took the biotransformation world scene as the predominant biocatalysts, a new, promising enzyme was discovered and characterized. The acyltransferase from Mycobacterium smegmatis (MsAcT) has in fact an extraordinary activity for a wide array of reactions, such as trans-esterification, amidation, trans-amidation and perhydrolysis, both in water and solvent media, giving rise to a series of interesting compounds including APIs (i.e., active pharmaceutical ingredients), natural flavors and fragrances, monomers for polymer synthesis, and peracids employed as disinfectants or antimicrobials. Although the most used acylating agent has been ethyl acetate (EtOAc), depending on the reaction type also acetamide, dimethyl carbonate and a variety of other esters, have been reported. The best yields were reached using very reactive donors such as vinyl or isopropenyl esters (almost complete conversion in rapid reaction times and water media for condensation reactions). In this review article the most innovative scientific advances on MsAcT, its mechanism and engineering are summarized, putting a particular focus on the different kind of processes (batch and flow) that it is possible to carry out using this enzyme as free or immobilized form. In conclusion, the author personal view on the unexplored reaction possibilities using MsAcT is reported as a window on the future of the topic.

Keywords: Condensation reaction; Enzyme engineering; Enzyme immobilization; Flow chemistry; Green and sustainable chemistry; Mycobacterium smegmatis acyltransferase (MsAcT); Perhydrolysis reaction.

Publication types

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

MeSH terms

  • Acyltransferases* / metabolism
  • Biocatalysis
  • Enzymes, Immobilized / metabolism
  • Esterification
  • Esters
  • Mycobacterium smegmatis* / metabolism
  • Water

Substances

  • Enzymes, Immobilized
  • Esters
  • Water
  • Acyltransferases