ArticleApplied and environmental microbiology2015
Three New Cutinases from the Yeast Arxula adeninivorans That Are Suitable for Biotechnological Applications.
Article in Applied and environmental microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 32 citations in OpenAlex.
- High-Level Expression of Humicola insolens Cutinase in Bacillus subtilis.Applied biochemistry and biotechnology · 2025Article
- Biochemical Characterization and Polyester-Binding/Degrading Capability of Two Cutinases fromMicroorganisms · 2025Article
- Discovery of two novel cutinases from a gut yeast of plastic-eating mealworm for polyester depolymerization.Applied and environmental microbiology · 2025Article
- Adaptation of yeast Saccharomyces cerevisiae to grape-skin environment.Scientific reports · 2023Article
- A Review of the Fungi That Degrade Plastic.Journal of fungi (Basel, Switzerland) · 2022Review
- Cutinase ACut2 fromMicroorganisms · 2022Article
- Development of a Vector Set for High or Inducible Gene Expression and Protein Secretion in the Yeast GenusJournal of fungi (Basel, Switzerland) · 2022Article
- Phylogenetic analysis and in-depth characterization of functionally and structurally diverse CE5 cutinases.The Journal of biological chemistry · 2021Article
- Structural Insight into a Yeast Maltase-TheJournal of fungi (Basel, Switzerland) · 2021Article
- Yeasts of the Blastobotrys genus are promising platform for lipid-based fuels and oleochemicals production.Applied microbiology and biotechnology · 2021Review
- High-level expression and characterization of a novel cutinase fromBiotechnology for biofuels · 2017Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The genes ACUT1, ACUT2, and ACUT3, encoding cutinases, were selected from the genomic DNA of Arxula adeninivorans LS3. The alignment of the amino acid sequences of these cutinases with those of other cutinases or cutinase-like enzymes from different fungi showed that they all had a catalytic S-D-H triad with a conserved G-Y-S-Q-G domain. All three genes were overexpressed in A. adeninivorans using the strong constitutive TEF1 promoter. Recombinant 6× His (6h)-tagged cutinase 1 protein (p) from A. adeninivorans LS3 (Acut1-6hp), Acut2-6hp, and Acut3-6hp were produced and purified by immobilized-metal ion affinity chromatography and biochemically characterized using p-nitrophenyl butyrate as the substrate for standard activity tests. All three enzymes from A. adeninivorans were active from pH 4.5 to 6.5 and from 20 to 30°C. They were shown to be unstable under optimal reaction conditions but could be stabilized using organic solvents, such as polyethylene glycol 200 (PEG 200), isopropanol, ethanol, or acetone. PEG 200 (50%, vol/vol) was found to be the best stabilizing agent for all of the cutinases, and acetone greatly increased the half-life and enzyme activity (up to 300% for Acut3-6hp). The substrate spectra for Acut1-6hp, Acut2-6hp, and Acut3-6hp were quite similar, with the highest activity being for short-chain fatty acid esters of p-nitrophenol and glycerol. Additionally, they were found to have polycaprolactone degradation activity and cutinolytic activity against cutin from apple peel. The activity was compared with that of the 6× His-tagged cutinase from Fusarium solani f. sp. pisi (FsCut-6hp), also expressed in A. adeninivorans, as a positive control. A fed-batch cultivation of the best Acut2-6hp-producing strain, A. adeninivorans G1212/YRC102-ACUT2-6H, was performed and showed that very high activities of 1,064 U ml(-1) could be achieved even with a nonoptimized cultivation procedure.
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