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Selective production of deacetylated mannosylerythritol lipid, MEL-D, by acetyltransferase disruption mutant of Pseudozyma hubeiensis.
Konishi, Masaaki; Makino, Motoki.
Affiliation
  • Konishi M; Department of Biotechnology and Environmental Chemistry, Kitami Institute of Technology, 165 Koen-cho, Kitami, Hokkaido 090-8507, Japan. Electronic address: konishim@mail.kitami-it.ac.jp.
  • Makino M; Department of Biotechnology and Environmental Chemistry, Kitami Institute of Technology, 165 Koen-cho, Kitami, Hokkaido 090-8507, Japan.
J Biosci Bioeng ; 125(1): 105-110, 2018 Jan.
Article in En | MEDLINE | ID: mdl-28847576
Mannosylerythritol lipids (MELs) are produced by several smut fungi of the Ustilaginaceae family; they are promising microbial biosurfactants and have excellent surface-active and self-assembling properties. Pseudozyma hubeiensis is a candidate for abundant MEL production and produces large amounts of 4-O-[(4'-mono-O-acetyl-2',3'-di-O-alkanoyl)-ß-d-mannopyranosyl]-meso-erythritol (MEL-C). An acetyltransferase disruption mutant of P. hubeiensis, SY62-MM36, was obtained to selectively produce deacetylated 4-O-[(2',3'-di-O-alkanoyl)-ß-d-mannopyranosyl]-meso-erythritol (MEL-D), and the structures of the products were determined. Lower mobility of major spots of the mutant on silica gel thin-layer chromatography verified its more hydrophilic nature than that of wild-type MEL-A, B, and C. Structural analyses confirmed the product to be MEL-D, which comprises acyl chains of caproic acid (C6:0), capric acid (C10:0), and lauric acid (C12:0). The critical micelle concentration (CMC) and the surface tension (γCMC) of the MEL-D were 2.0 × 10-5 M and 29.7 mN/m, respectively. SY62-MM36 also produced a minor product that was estimated as triacylated MEL-D. The triacylated MEL-D had a CMC of 3.5 × 10-5 M and a γCMC of 29.6 mN/m. In water, MEL-D formed a lamella liquid crystal phase over a broad range of concentrations. By fed-batch cultivation, the mutant produced 91.6 ± 6.3 g/L of MEL-D for 7 days.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Acetyltransferases / Ustilaginales / Glycolipids Language: En Journal: J Biosci Bioeng Journal subject: ENGENHARIA BIOMEDICA / MICROBIOLOGIA Year: 2018 Document type: Article Country of publication: Japan

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Acetyltransferases / Ustilaginales / Glycolipids Language: En Journal: J Biosci Bioeng Journal subject: ENGENHARIA BIOMEDICA / MICROBIOLOGIA Year: 2018 Document type: Article Country of publication: Japan