Isolation of Yeast<i>Kurtzmanomyces</i>sp. I-11, Novel Producer of Mannosylerythritol Lipid

Kakugawa, Koji; Tamai, Masamitsu; Imamura, Kunihiko; Miyamoto, Κ.; Miyoshi, Shozo; Morinaga, Yuki; Сузукі, Осаму; Miyakawa, Tokichi

doi:10.1271/bbb.66.188

Cited by 55 publications

(21 citation statements)

References 14 publications

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“…Depending on the number of acetyl groups, mannosylerythritol lipids can be differentiated into MEL A (fully acetylated), MEL B and MEL C (monoacetylated at R-6 and R-4, respectively), and the fully deacetylated MEL D (18). Mannosylerythritol-containing lipids have been identified in a variety of fungal species, e.g., Schizonella melanogramma, Candida antarctica, Kurtzmanomyces sp., and Pseudozyma aphidis (5,15,18,27). Besides their high surface activity, mannosylerythritol lipids display interesting biological activities.…”

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confidence: 99%

Identification of a Gene Cluster for Biosynthesis of Mannosylerythritol Lipids in the Basidiomycetous Fungus Ustilago maydis

Hewald

Linne

Scherer

et al. 2006

Appl Environ Microbiol

142

135

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Many microorganisms produce surface-active substances that enhance the availability of water-insoluble substrates. Although many of these biosurfactants have interesting potential applications, very little is known about their biosynthesis. The basidiomycetous fungus Ustilago maydis secretes large amounts of mannosylerythritol lipids (MELs) under conditions of nitrogen starvation. We recently described a putative glycosyltransferase, Emt1, which is essential for MEL biosynthesis and whose expression is strongly induced by nitrogen limitation. We used DNA microarray analysis to identify additional genes involved in MEL biosynthesis. Here we show that emt1 is part of a gene cluster which comprises five open reading frames. Three of the newly identified proteins, Mac1, Mac2, and Mat1, contain short sequence motifs characteristic for acyl-and acetyltransferases. Mutational analysis revealed that Mac1 and Mac2 are essential for MEL production, which suggests that they are involved in the acylation of mannosylerythritol. Deletion of mat1 resulted in the secretion of completely deacetylated MELs, as determined by mass spectrometry. We overexpressed Mat1 in Escherichia coli and demonstrated that this enzyme acts as an acetyl coenzyme A-dependent acetyltransferase. Remarkably, Mat1 displays relaxed regioselectivity and is able to acetylate mannosylerythritol at both the C-4 and C-6 hydroxyl groups. Based on these results, we propose a biosynthesis pathway for the generation of mannosylerythritol lipids in U. maydis.

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confidence: 99%

Identification of a Gene Cluster for Biosynthesis of Mannosylerythritol Lipids in the Basidiomycetous Fungus Ustilago maydis

Hewald

Linne

Scherer

et al. 2006

Appl Environ Microbiol

142

135

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“…I-11 as a high level producer of mannosylerythritol lipid (MEL). 10) This strain produces MEL when the cells are grown in a medium containing soybean oil as a sole carbon source. During the initial phase of cultivation, the pH of the culture broth dropped to 3.2 and the soybean oil was rapidly hydrolyzed to the fatty acid and the glycerol at that pH, suggesting that acidophilic lipase(s) was produced in the culture broth.…”

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Purification and Characterization of a Lipase from the Glycolipid-Producing YeastKurtzmanomycessp. I-11

Kakugawa

Shobayashi

Сузукі

et al. 2002

Bioscience, Biotechnology, and Biochemistry

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An extracellular lipase produced by the glycolipidproducing yeast Kurtzmanomyces sp. I-11 was puriˆed by ammonium sulfate precipitation and column chromatographies on DEAE-Sephadex A-25, SP-Sephadex C-50, and Sephadex G-100. Based on the analysis of the puriˆed lipase on sodium dodecyl sulfatepolyacrylamide gel electrophoresis, the puriˆed lipase was judged to be homogeneous and its molecular mass was estimated to be approximately 49 kDa. The optimum temperature for the activity was 759 C, and the activity was very stable at temperatures below 709 C. The active pH range of this lipase was 1.9-7.2, and the activity was stable at pH below 7.1. The lipase showed a preference for C18 acyl groups by measurements with pnitrophenyl esters and triglycerides as substrates. The lipase was very stable in the presence of various organic solvents at a concentration of 40z. Although the Nterminal sequence of the Kurtzmanomyces lipase was very similar to that of lipase A from Candida antarctica, the pH proˆles of the two lipases were signiˆcantly diŠerent.

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“…I-11 produces a novel MEL composed of a sugar moiety, 6-Ob-D-mannopyranosyl-(1!4)-O-meso-erythritol, and a mixture of fatty acids [C 8:0 (36.4%), C 12:0 (11.9%) and C 14:2 (25.9)] (Kakugawa et al 2002) as the lipophilic group. C. antarctica KCTC 7804, which is isolated from an oil-contaminated site, produced a MEL containing 6-O-acetyl-2,3-di-O-alkanoyl-b-D-mannopyranosyl-(1!4)-O-meso-erythritol.…”

Section: Mel-a Producersmentioning

confidence: 99%

“…(as a major component) (Kitamoto et al 1990a, b), Kurtzmanomyces sp. (Kakugawa et al 2002), and different strains of the genus Candida. The synthesis of MEL is not growth-associated, and it can also be produced by using resting (stationary phase) cells of yeast.…”

Section: Introductionmentioning

confidence: 99%

Mannosylerythritol Lipids: Microbial Production and Their Applications

Arutchelvi

Doble

2010

Microbiology Monographs

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Isolation of YeastKurtzmanomycessp. I-11, Novel Producer of Mannosylerythritol Lipid

Cited by 55 publications

References 14 publications

Identification of a Gene Cluster for Biosynthesis of Mannosylerythritol Lipids in the Basidiomycetous Fungus Ustilago maydis

Identification of a Gene Cluster for Biosynthesis of Mannosylerythritol Lipids in the Basidiomycetous Fungus Ustilago maydis

Purification and Characterization of a Lipase from the Glycolipid-Producing YeastKurtzmanomycessp. I-11

Mannosylerythritol Lipids: Microbial Production and Their Applications

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