ArticleApplied and environmental microbiology2009
Novel Coprinopsis cinerea polyesterase that hydrolyzes cutin and suberin.
Article in Applied and environmental microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 55 citations in OpenAlex.
- Visualization of Suberization and Lignification in Sugarcane.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Hydrophobic cell surface display system of PETase as a sustainable biocatalyst for PET degradation.Frontiers in microbiology · 2022Article
- Enzymatic Bioprospecting of Fungi Isolated from a Tropical Rainforest in Mexico.Journal of fungi (Basel, Switzerland) · 2021Article
- Phylogenetic analysis and in-depth characterization of functionally and structurally diverse CE5 cutinases.The Journal of biological chemistry · 2021Article
- Enzymatic Degradation of p-Nitrophenyl Esters, Polyethylene Terephthalate, Cutin, and Suberin by Sub1, a Suberinase Encoded by the Plant Pathogen Streptomyces scabies.Microbes and environments · 2020Article
- Article
- High-level expression and characterization of a novel cutinase fromBiotechnology for biofuels · 2017Article
- Proteome Analyses of Soil Bacteria Grown in the Presence of Potato Suberin, a Recalcitrant Biopolymer.Microbes and environments · 2016Article
- Physical, Chemical and Proteomic Evidence of Potato Suberin Degradation by the Plant Pathogenic Bacterium Streptomyces scabiei.Microbes and environments · 2016Article
- Genome wide analysis of protein production load in Trichoderma reesei.Biotechnology for biofuels · 2016Article
- Three New Cutinases from the Yeast Arxula adeninivorans That Are Suitable for Biotechnological Applications.Applied and environmental microbiology · 2015Article
- Elucidating how the saprophytic fungus Aspergillus nidulans uses the plant polyester suberin as carbon source.BMC genomics · 2014Article
- Comparative secretome analysis of Streptomyces scabiei during growth in the presence or absence of potato suberin.Proteome science · 2014Article
- Two novel class II hydrophobins from Trichoderma spp. stimulate enzymatic hydrolysis of poly(ethylene terephthalate) when expressed as fusion proteins.Applied and environmental microbiology · 2013Article
- The wood rot ascomycete Xylaria polymorpha produces a novel GH78 glycoside hydrolase that exhibits α-L-rhamnosidase and feruloyl esterase activities and releases hydroxycinnamic acids from lignocelluloses.Applied and environmental microbiology · 2012Article
- Potato suberin induces differentiation and secondary metabolism in the genus Streptomyces.Microbes and environments · 2012Article
- Secreted fungal sulfhydryl oxidases: sequence analysis and characterisation of a representative flavin-dependent enzyme from Aspergillus oryzae.BMC biochemistry · 2010Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Three cutinase gene-like genes from the basidiomycete Coprinopsis cinerea (Coprinus cinereus) found with a similarity search were cloned and expressed in Trichoderma reesei under the control of an inducible cbh1 promoter. The selected transformants of all three polyesterase constructs showed activity with p-nitrophenylbutyrate, used as a model substrate. The most promising transformant of the cutinase CC1G_09668.1 gene construct was cultivated in a laboratory fermentor, with a production yield of 1.4 g liter(-l) purified protein. The expressed cutinase (CcCUT1) was purified to homogeneity by immobilized metal affinity chromatography exploiting a C-terminal His tag. The N terminus of the enzyme was found to be blocked. The molecular mass of the purified enzyme was determined to be around 18.8 kDa by mass spectrometry. CcCUT1 had higher activity on shorter (C(2) to C(10)) fatty acid esters of p-nitrophenol than on longer ones, and it also exhibited lipase activity. CcCUT1 had optimal activity between pH 7 and 8 but retained activity over a wide pH range. The enzyme retained 80% of its activity after 20 h of incubation at 50 degrees C, but residual activity decreased sharply at 60 degrees C. Microscopic analyses and determination of released hydrolysis products showed that the enzyme was able to depolymerize apple cutin and birch outer bark suberin.
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