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Characterization of sophorolipid biosynthetic enzymes from Starmerella bombicola

Karen Saerens (UGent) , Inge Van Bogaert (UGent) and Wim Soetaert (UGent)
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Abstract
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.
Keywords
IDENTIFICATION, CANDIDA-BOMBICOLA, CHROMATOGRAPHY, GLUCOSYLTRANSFERASES, LIPIDS, GLYCOLIPIDS, BOGORIENSIS, ACID, ATCC 22214, glucosyltransferase, sophorolipid biosynthesis, acetyltransferase, CASTOR-OIL, biosurfactants, glycolipid, Starmerella bombicola

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Citation

Please use this url to cite or link to this publication:

Chicago
Saerens, Karen, Inge Van Bogaert, and Wim Soetaert. 2015. “Characterization of Sophorolipid Biosynthetic Enzymes from Starmerella Bombicola.” Fems Yeast Research 15 (7).
APA
Saerens, K., Van Bogaert, I., & Soetaert, W. (2015). Characterization of sophorolipid biosynthetic enzymes from Starmerella bombicola. FEMS YEAST RESEARCH, 15(7).
Vancouver
1.
Saerens K, Van Bogaert I, Soetaert W. Characterization of sophorolipid biosynthetic enzymes from Starmerella bombicola. FEMS YEAST RESEARCH. 2015;15(7).
MLA
Saerens, Karen, Inge Van Bogaert, and Wim Soetaert. “Characterization of Sophorolipid Biosynthetic Enzymes from Starmerella Bombicola.” FEMS YEAST RESEARCH 15.7 (2015): n. pag. Print.
@article{8029442,
  abstract     = {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.},
  author       = {Saerens, Karen and Van Bogaert, Inge and Soetaert, Wim},
  issn         = {1567-1356},
  journal      = {FEMS YEAST RESEARCH},
  language     = {eng},
  number       = {7},
  pages        = {9},
  title        = {Characterization of sophorolipid biosynthetic enzymes from Starmerella bombicola},
  url          = {http://dx.doi.org/10.1093/femsyr/fov075},
  volume       = {15},
  year         = {2015},
}

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