Bacterial acyltransferases as an alternative for lipase-catalyzed acylation for the production of oleochemicals and fuels.
Bacterial acyltransferases are a new class of enzymes, and the first member was identified as WS/DGAT in Acinetobacter baylyi ADP1. Their unspecificity have been used in several biotechnological applications for lipid modification, a field that has been dominated by the use of lipases. Examples are the biosynthesis of jojoba-like wax esters and fatty-acid ethyl esters. In addition, these enzymes are also capable of synthesizing acylthioesters. Acyloxoesters and acylthioesters can thus be produced in vivo by whole-cell fermentations rather than in vitro in an enzyme reactor. In this Minireview, we focus on the biotechnological utilization of acyltransferases for the production of modified lipids from renewable resources.
Stöveken
Tim
T
Institut für Molekulare Mikrobiologie und Biotechnologie, Westfälische Wilhelms-Universität Münster, Corrensstr. 3, 48149 Münster, Germany.
Steinbüchel
Alexander
A
D000150:Acinetobacter / Q000201:enzymology; D000215:Acylation; D000217:Acyltransferases / Q000737:chemistry* / Q000145:classification; D020816:Amino Acid Motifs; D001426:Bacterial Proteins / Q000737:chemistry* / Q000145:classification; D001665:Binding Sites; D007218:Industrial Microbiology / Q000379:methods*; D008049:Lipase / Q000737:chemistry; D008055:Lipids / Q000096:biosynthesis*
D001426:Bacterial Proteins; D008055:Lipids; D000217:Acyltransferases; D008049:Lipase