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Saerens KM, Zhang J, Saey L, Van Bogaert IN, Soetaert W
Cloning and functional characterization of the UDP-glucosyltransferase UgtB1 involved in sophorolipid production by Candida bombicola and creation of a glucolipid-producing yeast strain
Yeast 28(4) (2011)
279–292
Candida bombicola B11
(later renamed to: Starmerella bombicola B11)
(Ancestor NCBI TaxID 75736,
species name lookup)
Taxonomic group: fungi / Ascomycota
(Phylum: Ascomycota)
NCBI PubMed ID: 21456054Publication DOI: 10.1002/yea.1838Journal NLM ID: 8607637Publisher: Chichester, Wiley
Correspondence: Saerens KM <Karen.Saerens
UGent.be>
Institutions: Laboratory of Industrial Biotechnology and Biocatalysis, Faculty of Bioscience Engineering, Ghent University, Ghent,Belgium
Sophorolipids produced by the non-pathogenic yeast Candida bombicola ATCC 22214 are glycolipid biosurfactants applied commercially as biodegradable and eco-friendly detergents. Their low cell toxicity, excellent wetting capability and antimicrobial activity attract the attention of high-value markets, such as the cosmetic and pharmaceutical industries. Although sophorolipid production yields have been increased by the optimization of fermentation parameters and feed sources, the biosynthetic pathway and genetic mechanism behind sophorolipid production still remains unclear. Here we identify a UDP-glucosyltransferase gene, UGTB1, with a key function in this economically important pathway. The protein shows sequence and structural homology to several bacterial glycosyltransferases involved in macrolide antibiotic synthesis. Deletion of UGTB1 in C. bombicola did not affect cell growth and resulted in a yeast producing glucolipids, thereby opening the route for in vivo production of these glycolipid intermediates. Activity assays on cell lysates confirmed that the identified gene is responsible for the second glucosylation step during sophorolipid production and illustrated that sophorolipid production in C. bombicola involves the stepwise action of two independent glucosyltransferases. The complete UGTB1 sequence data have been submitted to the GenBank database (http://www.ncbi.nlm.nih.gov) under Accession No. HM440974.
glucosyltransferase, biosurfactant, sophorolipid, Candida bombicola, glucolipid
Structure type: monomer ; 460 [M+H]+
Location inside paper: fig. 4, fig. 7 (first bottom structure)
Compound class: glucolipid
Contained glycoepitopes: IEDB_142488,IEDB_146664,IEDB_983931,SB_192
Methods: DNA techniques, MS, HPLC, extraction, GC–MS
Synthetic data: enzymatic
Comments, role: This is one of the three predominant mono-acetylated acidic glucolipids that was found in a C. bombicola B11 mutant culture extract 14 days after cultivation on rapeseed oil. This sophorolipid is produced in interaction between UDP-glucose and fatty acid.
Related record ID(s): 43557, 43592, 43593
NCBI Taxonomy refs (TaxIDs): 75736
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Saerens KM, Zhang J, Saey L, Van Bogaert IN, Soetaert W
Cloning and functional characterization of the UDP-glucosyltransferase UgtB1 involved in sophorolipid production by Candida bombicola and creation of a glucolipid-producing yeast strain
Yeast 28(4) (2011)
279–292
Candida bombicola B11
(later renamed to: Starmerella bombicola B11)
(Ancestor NCBI TaxID 75736,
species name lookup)
Taxonomic group: fungi / Ascomycota
(Phylum: Ascomycota)
NCBI PubMed ID: 21456054Publication DOI: 10.1002/yea.1838Journal NLM ID: 8607637Publisher: Chichester, Wiley
Correspondence: Saerens KM <Karen.Saerens
UGent.be>
Institutions: Laboratory of Industrial Biotechnology and Biocatalysis, Faculty of Bioscience Engineering, Ghent University, Ghent,Belgium
Sophorolipids produced by the non-pathogenic yeast Candida bombicola ATCC 22214 are glycolipid biosurfactants applied commercially as biodegradable and eco-friendly detergents. Their low cell toxicity, excellent wetting capability and antimicrobial activity attract the attention of high-value markets, such as the cosmetic and pharmaceutical industries. Although sophorolipid production yields have been increased by the optimization of fermentation parameters and feed sources, the biosynthetic pathway and genetic mechanism behind sophorolipid production still remains unclear. Here we identify a UDP-glucosyltransferase gene, UGTB1, with a key function in this economically important pathway. The protein shows sequence and structural homology to several bacterial glycosyltransferases involved in macrolide antibiotic synthesis. Deletion of UGTB1 in C. bombicola did not affect cell growth and resulted in a yeast producing glucolipids, thereby opening the route for in vivo production of these glycolipid intermediates. Activity assays on cell lysates confirmed that the identified gene is responsible for the second glucosylation step during sophorolipid production and illustrated that sophorolipid production in C. bombicola involves the stepwise action of two independent glucosyltransferases. The complete UGTB1 sequence data have been submitted to the GenBank database (http://www.ncbi.nlm.nih.gov) under Accession No. HM440974.
glucosyltransferase, biosurfactant, sophorolipid, Candida bombicola, glucolipid
Structure type: monomer ; 502 [M+H]+
Location inside paper: fig. 7 (top structure)
Compound class: glucolipid
Contained glycoepitopes: IEDB_142488,IEDB_146664,IEDB_983931,SB_192
Methods: DNA techniques, MS, HPLC, extraction, GC–MS
Comments, role: This is one of the three predominant mono-acetylated acidic glucolipids that was found in a C. bombicola B11 mutant culture extract 14 days after cultivation on rapeseed oil.
Related record ID(s): 43557, 43591, 43593
NCBI Taxonomy refs (TaxIDs): 75736
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There is only one chemically distinct structure:
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Saerens KM, Zhang J, Saey L, Van Bogaert IN, Soetaert W
Cloning and functional characterization of the UDP-glucosyltransferase UgtB1 involved in sophorolipid production by Candida bombicola and creation of a glucolipid-producing yeast strain
Yeast 28(4) (2011)
279–292
Candida bombicola B11
(later renamed to: Starmerella bombicola B11)
(Ancestor NCBI TaxID 75736,
species name lookup)
Taxonomic group: fungi / Ascomycota
(Phylum: Ascomycota)
NCBI PubMed ID: 21456054Publication DOI: 10.1002/yea.1838Journal NLM ID: 8607637Publisher: Chichester, Wiley
Correspondence: Saerens KM <Karen.Saerens
UGent.be>
Institutions: Laboratory of Industrial Biotechnology and Biocatalysis, Faculty of Bioscience Engineering, Ghent University, Ghent,Belgium
Sophorolipids produced by the non-pathogenic yeast Candida bombicola ATCC 22214 are glycolipid biosurfactants applied commercially as biodegradable and eco-friendly detergents. Their low cell toxicity, excellent wetting capability and antimicrobial activity attract the attention of high-value markets, such as the cosmetic and pharmaceutical industries. Although sophorolipid production yields have been increased by the optimization of fermentation parameters and feed sources, the biosynthetic pathway and genetic mechanism behind sophorolipid production still remains unclear. Here we identify a UDP-glucosyltransferase gene, UGTB1, with a key function in this economically important pathway. The protein shows sequence and structural homology to several bacterial glycosyltransferases involved in macrolide antibiotic synthesis. Deletion of UGTB1 in C. bombicola did not affect cell growth and resulted in a yeast producing glucolipids, thereby opening the route for in vivo production of these glycolipid intermediates. Activity assays on cell lysates confirmed that the identified gene is responsible for the second glucosylation step during sophorolipid production and illustrated that sophorolipid production in C. bombicola involves the stepwise action of two independent glucosyltransferases. The complete UGTB1 sequence data have been submitted to the GenBank database (http://www.ncbi.nlm.nih.gov) under Accession No. HM440974.
glucosyltransferase, biosurfactant, sophorolipid, Candida bombicola, glucolipid
Structure type: monomer
Location inside paper: fig. 7
Compound class: glucolipid
Contained glycoepitopes: IEDB_142488,IEDB_146664,IEDB_983931,SB_192
Methods: DNA techniques, MS, HPLC, extraction, GC–MS
Comments, role: This sophorolipid is produced by interaction between UDP-glucose and glucolipid. This reaction used for detection GTII activity.
Related record ID(s): 43557, 43591, 43592
NCBI Taxonomy refs (TaxIDs): 75736
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Delbeke EIP, Van Geem KM, Stevens CV, Van Bogaert INA
Sophorolipid modification: the power of yeasts and enzymes
Book: Lipid modification by enzymes and engineered microbes (2018)
Vol. 1, Chapter 14, 315-341
|
b-D-Glcp-(1-7)-Subst
Subst = pentadecan-7-ol = SMILES CCCCCCCC{7}C(O)CCCCCC |
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Starmerella bombicola
(NCBI TaxID 75736,
species name lookup)
Taxonomic group: fungi / Ascomycota
(Phylum: Ascomycota)
Publication DOI: 10.1016/B978-0-12-813167-1.00014-1Publisher: N.J.: Academic Press and AOCS Press
Editors: Bornscheuer UT
Institutions: SynBioC, Ghent University, Ghent, Belgium, LCT, Ghent University, Ghent, Belgium, Centre for Synthetic Biology, Ghent University, Ghent, Belgium
Sophorolipids are biosurfactants or biological detergents composed of a hydroxylated fatty acid and the glucose disaccharide sophorose. These commercially relevant molecules are produced by the yeast Starmerella bombicola and offer a green and renewable alternative for traditional surfactants.To further broaden up the application potential of sophorolipids, introduction of structural variation is essential as this influences their physicochemical and biological properties. However, creating molecular variants is not as straightforward as for petrochemically derived surfactants. This is, on the one hand, a consequence of the biological origin and restricting biochemistry behind it, and is, on the other hand, caused by the complexity of chemical processes regarding the necessity of protection and deprotection of the glucose units.In this chapter, several strategies to overcome these limitations will be discussed, such as the use of special substrates during yeast cultivation, design of engineered strains, and enzymatic modification.
enzymatic modification, yeast, sophorolipid, Starmerella bombicola, lipase, Novozym 435, strain engineering
Structure type: monomer
Location inside paper: Fig. 14.5(20)
Compound class: glucolipid
Contained glycoepitopes: IEDB_142488,IEDB_146664,IEDB_983931,SB_192
Enzymes that release or process the structure: CYP52M1, UGTA1, UGTB1, AT, SL ABC
Synthetic data: enzymatic in vivo
Comments, role: review; generated in presence of 2-hexyl-1-dodecanol
Related record ID(s): 48829, 48830, 48831, 48832, 48834, 48835, 48836, 48837, 48838, 48839, 48840, 48841, 48842, 48843, 48844, 48845, 48846, 48847, 48848, 48849, 48850, 48851, 48852, 48977, 48985, 48986, 48987, 48990
NCBI Taxonomy refs (TaxIDs): 75736
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There is only one chemically distinct structure:
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