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Defining Substrate Specificities for Lipase and Phospholipase Candidates

Defining Substrate Specificities for Lipase and Phospholipase Candidates

Published on: November 23, 2016

Differences in substrate specificities of five bacterial wax ester synthases.

Brett M Barney¹, Bradley D Wahlen, EmmaLee Garner

¹Department of Bioproducts and Biosystems Engineering, University of Minnesota, St. Paul, Minnesota, USA. bbarney@umn.edu

Applied and Environmental Microbiology

|June 12, 2012

Summary

Researchers characterized wax ester synthase/diacylglycerol acyltransferase (WS/DGAT) enzymes from four bacteria. One enzyme from Marinobacter aquaeolei VT8 showed high activity, indicating potential for biofuel production.

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Area of Science:

Microbiology
Biochemistry
Biotechnology

Background:

Wax esters serve as carbon and energy storage in bacteria.
The bifunctional wax ester synthase/acyl-coenzyme A (acyl-CoA):diacylglycerol acyltransferase (WS/DGAT) enzyme catalyzes wax ester synthesis.

Purpose of the Study:

To isolate and characterize five WS/DGAT enzymes from four bacterial species.
To investigate the substrate range and kinetic properties of these enzymes.
To correlate in vitro enzyme activity with in vivo product profiles for biotechnological applications.

Main Methods:

Isolation and purification of WS/DGAT enzymes.
Kinetic studies to determine substrate specificity and activity.
Analysis of wax ester and triacylglyceride profiles in bacteria grown under lipid-accumulating conditions.

Main Results:

Differential enzyme activity observed based on substrate addition order and enzyme source.
Subtle differences in substrate selectivity among the characterized WS/DGAT enzymes.
Marinobacter aquaeolei VT8 WS/DGAT exhibited significantly higher activity and easier purification.

Conclusions:

WS/DGAT enzymes play a role in determining bacterial wax ester profiles under nutrient stress.
The M. aquaeolei VT8 WS/DGAT enzyme shows promise for biotechnological applications.
Further research can explore these enzymes for producing biofuels and high-value petrochemicals.