Bacterial Acyltransferases as an Alternative for Lipase-Catalyzed Acylation for the Production of Oleochemicals and Fuels
✍ Scribed by Tim Stöveken; Alexander Steinbüchel
- Publisher
- John Wiley and Sons
- Year
- 2008
- Tongue
- English
- Weight
- 973 KB
- Volume
- 47
- Category
- Article
- ISSN
- 0044-8249
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✦ Synopsis
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.
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## Abstract Candida antarctica __lipase B (CAL‐B) catalyzes the regioselective acylation of natural thymidine with oxime esters and also the regioselective acylation of an analogue, 3′,5′‐diamino‐3′,5′‐dideoxythymidine with nonactivated esters. In both cases, acylation favors the less hindered 5′‐p