Dataset Information

Structural and Biochemical Studies of a Biocatalyst for the Enzymatic Production of Wax Esters.

ABSTRACT: Wax esters are high-value products whose enzymatic synthesis is of increasing biotechnological interest. The fabrication of cell factories that mass-produce wax esters may provide a facile route towards a sustainable, and environment-friendly approach to a large-scale process for this commodity chemical. An expedient route for wax-ester biocatalysis may be facilitated by the action of enzymes termed wax ester synthases/diacylglycerol acyltransferases (WS/DGAT), which produce wax esters using fatty acids and alcohols as a precursor. In this work, we report the structure for a member of the WS/DGAT superfamily. The structural data in conjunction with bioinformatics and mutational analyses allowed us to identify the substrate binding pockets, and residues that may be important for catalysis. Using this information as a guide, we generated a mutant with preference towards shorter acyl-substrates. This study demonstrates the efficacy of a structure-guided engineering effort towards a WS/DGAT variant with preference towards wax esters of desired lengths.

SUBMITTER: Petronikolou N

PROVIDER: S-EPMC6761989 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Structural and Biochemical Studies of a Biocatalyst for the Enzymatic Production of Wax Esters.

Petronikolou Nektaria N Nair Satish K SK

ACS catalysis 20180601 7

Wax esters are high-value products whose enzymatic synthesis is of increasing biotechnological interest. The fabrication of cell factories that mass-produce wax esters may provide a facile route towards a sustainable, and environment-friendly approach to a large-scale process for this commodity chemical. An expedient route for wax-ester biocatalysis may be facilitated by the action of enzymes termed wax ester synthases/diacylglycerol acyltransferases (WS/DGAT), which produce wax esters using fat ...[more]

PMID: 31559109

Similar Datasets

Project description:BackgroundSimmondsia chinensis (jojoba) is the only plant known to store wax esters instead of triacylglycerols in its seeds. Wax esters are composed of very-long-chain monounsaturated fatty acids and fatty alcohols and constitute up to 60% of the jojoba seed weight. During jojoba germination, the first step of wax ester mobilization is catalyzed by lipases. To date, none of the jojoba lipase-encoding genes have been cloned and characterized. In this study, we monitored mobilization of storage reserves during germination of jojoba seeds and performed detailed characterization of the jojoba lipases using microsomal fractions isolated from germinating seeds.ResultsDuring 26 days of germination, we observed a 60-70% decrease in wax ester content in the seeds, which was accompanied by the reduction of oleosin amounts and increase in glucose content. The activity of jojoba lipases in the seed microsomal fractions increased in the first 50 days of germination. The enzymes showed higher activity towards triacylglycerols than towards wax esters. The maximum lipase activity was observed at 60 °C and pH around 7 for triacylglycerols and 6.5-8 for wax esters. The enzyme efficiently hydrolyzed various wax esters containing saturated and unsaturated acyl and alcohol moieties. We also demonstrated that jojoba lipases possess wax ester-synthesizing activity when free fatty alcohols and different acyl donors, including triacylglycerols and free fatty acids, are used as substrates. For esterification reactions, the enzyme utilized both saturated and unsaturated fatty alcohols, with the preference towards long chain and very long chain compounds.ConclusionsIn in vitro assays, jojoba lipases catalyzed hydrolysis of triacylglycerols and different wax esters in a broad range of temperatures. In addition, the enzymes had the ability to synthesize wax esters in the backward reaction. Our data suggest that jojoba lipases may be more similar to other plant lipases than previously assumed.

Dataset Information

Structural and Biochemical Studies of a Biocatalyst for the Enzymatic Production of Wax Esters.

Publications

Structural and Biochemical Studies of a Biocatalyst for the Enzymatic Production of Wax Esters.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets