Characterization of sophorolipid biosynthetic enzymes from Starmerella bombicola

Altering glycolipid structure by genetic engineering of Starmerella bombicola is a recently started research topic and worthy alternative to the unsuccessful selective feeding strategies conventionally applied to reach this goal. One question to be addressed when expressing heterologous proteins in...

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Bibliographic Details
Published in:FEMS yeast research 2015-11, Vol.15 (7), p.fov075
Main Authors: Saerens, Karen M.J., Van Bogaert, Inge N.A., Soetaert, Wim
Format: Article
Language:English
Subjects:
Acetylation
Acetyltransferase
Acetyltransferases - metabolism
Deletion mutant
Enzymes
Fatty Acids - metabolism
Gene Expression Regulation, Enzymologic
Gene Expression Regulation, Fungal
Genetic engineering
Glucuronosyltransferase - metabolism
Glycolipids - biosynthesis
Intermediates
Saccharomycetales - genetics
Saccharomycetales - metabolism
Substrate Specificity
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Summary:Altering glycolipid structure by genetic engineering of Starmerella bombicola is a recently started research topic and worthy alternative to the unsuccessful selective feeding strategies conventionally applied to reach this goal. One question to be addressed when expressing heterologous proteins in S. bombicola is the activity of the subsequent biosynthetic enzymes toward such modified substrates. In this scope, we studied the substrate specificity of the UDP-glucosyltransferases UgtA1 and UgtB1, responsible for the stepwise synthesis of sophorolipids from a hydroxylated fatty acid, and that of the acetyltransferase, responsible for acetylation of the sophorolipid molecule. All enzymes showed specificity toward a C18:1 chained acceptor and both glucosyltransferases were highly selective toward the UDP-glucose donor. Severe product inhibition of the glucosyltransferases explains the limited accumulation of sophorolipid intermediates by earlier created single deletion mutants of S. bombicola. Finally, a more detailed study of the acetylation of sophorolipid intermediates sheds light on the enzymatic cascade during synthesis. Characterization of key enzymes involved in sophorolipid synthesis explains the difficulties in tailoring glycolipid structure by selective feeding or gene deletion and confirms the enzymatic cascade in the metabolic pathway.
ISSN:1567-1356
1567-1364
1567-1364
DOI:10.1093/femsyr/fov075