Evidence map›Paper›PMID 38937850›Full record

ArticleBiotechnology for biofuels and bioproducts2024

Revision of the sophorolipid biosynthetic pathway in Starmerella bombicola based on new insights in the substrate profile of its lactone esterase.

Zhoujian Diao, Sophie L K W Roelants, Goedele Luyten, Jan Goeman, Isabel Vandenberghe, Gonzalez Van Driessche, Sofie L De Maeseneire, Wim K Soetaert, Bart Devreese

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Article in Biotechnology for biofuels and bioproducts, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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3 · Its place in the literature

Who cites it

3 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Zhoujian DiaoLaboratory of Microbiology, Protein Research Unit, Department of Biochemistry and Microbiology, Faculty of Science, Ghent University, K. L. Ledeganckstraat 35, 9000, Ghent, Belgium.
Sophie L K W RoelantsDepartment of Biotechnology, Faculty of Bioscience Engineering, Centre for Industrial Biotechnology and Biocatalysis (InBio.Be), Ghent University, Coupure Links 653, 9000, Ghent, Belgium.
Goedele LuytenDepartment of Biotechnology, Faculty of Bioscience Engineering, Centre for Industrial Biotechnology and Biocatalysis (InBio.Be), Ghent University, Coupure Links 653, 9000, Ghent, Belgium.
Jan GoemanLaboratory for Organic and Bioorganic Synthesis, Department of Organic Chemistry, Ghent University, Krijgslaan 281 (S.4), 9000, Ghent, Belgium.
Isabel VandenbergheLaboratory of Microbiology, Protein Research Unit, Department of Biochemistry and Microbiology, Faculty of Science, Ghent University, K. L. Ledeganckstraat 35, 9000, Ghent, Belgium.
Gonzalez Van DriesscheLaboratory of Microbiology, Protein Research Unit, Department of Biochemistry and Microbiology, Faculty of Science, Ghent University, K. L. Ledeganckstraat 35, 9000, Ghent, Belgium.
Sofie L De MaeseneireDepartment of Biotechnology, Faculty of Bioscience Engineering, Centre for Industrial Biotechnology and Biocatalysis (InBio.Be), Ghent University, Coupure Links 653, 9000, Ghent, Belgium.
Wim K SoetaertDepartment of Biotechnology, Faculty of Bioscience Engineering, Centre for Industrial Biotechnology and Biocatalysis (InBio.Be), Ghent University, Coupure Links 653, 9000, Ghent, Belgium.
Bart DevreeseLaboratory of Microbiology, Protein Research Unit, Department of Biochemistry and Microbiology, Faculty of Science, Ghent University, K. L. Ledeganckstraat 35, 9000, Ghent, Belgium. Bart.Devreese@ugent.be.

Funding

Chinese Scholarship Council 201706150093Ghent University special research funds BOF21/CDV/064
6 · The paper itself

Abstract

backgroundSophorolipids (SLs) are a class of natural, biodegradable surfactants that found their way as ingredients for environment friendly cleaning products, cosmetics and nanotechnological applications. Large-scale production relies on fermentations using the yeast Starmerella bombicola that naturally produces high titers of SLs from renewable resources. The resulting product is typically an extracellular mixture of acidic and lactonic congeners. Previously, we identified an esterase, termed Starmerella bombicola lactone esterase (SBLE), believed to act as an extracellular reverse lactonase to directly use acidic SLs as substrate.

resultsWe here show based on newly available pure substrates, HPLC and mass spectrometric analysis, that the actual substrates of SBLE are in fact bola SLs, revealing that SBLE actually catalyzes an intramolecular transesterification reaction. Bola SLs contain a second sophorose attached to the fatty acyl group that acts as a leaving group during lactonization.

conclusionsThe biosynthetic function by which the Starmerella bombicola 'lactone esterase' converts acidic SLs into lactonic SLs should be revised to a 'transesterase' where bola SL are the true intermediate. This insights paves the way for alternative engineering strategies to develop designer surfactants.

Indexed as

BiosurfactantsBola sophorolipidsLactonic sophorolipidsLipaseMass spectrometrySerine hydrolaseStarmerella bombicola lactone esterase (SBLE)Transesterification

Identifiers

PMID38937850
PMCPMC11210130

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