Stoveken_2008_Angew.Chem.Int.Ed.Engl_47_3688

Reference

Title : Bacterial acyltransferases as an alternative for lipase-catalyzed acylation for the production of oleochemicals and fuels - Stoveken_2008_Angew.Chem.Int.Ed.Engl_47_3688
Author(s) : Stoveken T , Steinbuchel A
Ref : Angew Chem Int Ed Engl , 47 :3688 , 2008
Abstract :

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.

PubMedSearch : Stoveken_2008_Angew.Chem.Int.Ed.Engl_47_3688
PubMedID: 18399520

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Citations formats

Stoveken T, Steinbuchel A (2008)
Bacterial acyltransferases as an alternative for lipase-catalyzed acylation for the production of oleochemicals and fuels
Angew Chem Int Ed Engl 47 :3688

Stoveken T, Steinbuchel A (2008)
Angew Chem Int Ed Engl 47 :3688