Cutinase-like biodegradable plastic-degrading enzymes from phylloplane yeasts have cutinase activity
ABSTRACT Phylloplane yeast genera Pseudozyma and Cryptococcus secrete biodegradable plastic (BP)-degrading enzymes, termed cutinase-like enzymes (CLEs). Although CLEs contain highly conserved catalytic sites, the whole protein exhibits ≤30% amino acid sequence homology with cutinase. In this study,...
Published in: | Bioscience, Biotechnology, and Biochemistry |
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2021
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crinformauk:10.1093/bbb/zbab113 2024-09-15T17:44:13+00:00 Cutinase-like biodegradable plastic-degrading enzymes from phylloplane yeasts have cutinase activity Ueda, Hirokazu Tabata, Jun Seshime, Yasuyo Masaki, Kazuo Sameshima-Yamashita, Yuka Kitamoto, Hiroko Japan Society for the Promotion of Science Ministry of Education, Culture, Sports, Science and Technology Bio-oriented Technology Research Advancement Institution 2021 http://dx.doi.org/10.1093/bbb/zbab113 http://academic.oup.com/bbb/advance-article-pdf/doi/10.1093/bbb/zbab113/38983601/zbab113.pdf http://academic.oup.com/bbb/article-pdf/85/8/1890/39278541/zbab113.pdf en eng Informa UK Limited https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model Bioscience, Biotechnology, and Biochemistry volume 85, issue 8, page 1890-1898 ISSN 1347-6947 journal-article 2021 crinformauk https://doi.org/10.1093/bbb/zbab113 2024-08-05T04:23:54Z ABSTRACT Phylloplane yeast genera Pseudozyma and Cryptococcus secrete biodegradable plastic (BP)-degrading enzymes, termed cutinase-like enzymes (CLEs). Although CLEs contain highly conserved catalytic sites, the whole protein exhibits ≤30% amino acid sequence homology with cutinase. In this study, we analyzed whether CLEs exhibit cutinase activity. Seventeen Cryptococcus magnus strains, which degrade BP at 15 °C, were isolated from leaves and identified the DNA sequence of the CLE in one of the strains. Cutin was prepared from tomato leaves and treated with CLEs from 3 Cryptococcus species (C. magnus, Cryptococcus flavus, and Cryptococcus laurentii) and Pseudozyma antarctia (PaE). A typical cutin monomer, 10,16-dihydroxyhexadecanoic acid, was detected in extracts of the reaction solution via gas chromatography–mass spectrometry, showing that cutin was indeed degraded by CLEs. In addition to the aforementioned monomer, separation analysis via thin-layer chromatography detected high-molecular-weight products resulting from the breakdown of cutin by PaE, indicating that PaE acts as an endo-type enzyme. Article in Journal/Newspaper Antarc* Informa Bioscience, Biotechnology, and Biochemistry 85 8 1890 1898 |
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ABSTRACT Phylloplane yeast genera Pseudozyma and Cryptococcus secrete biodegradable plastic (BP)-degrading enzymes, termed cutinase-like enzymes (CLEs). Although CLEs contain highly conserved catalytic sites, the whole protein exhibits ≤30% amino acid sequence homology with cutinase. In this study, we analyzed whether CLEs exhibit cutinase activity. Seventeen Cryptococcus magnus strains, which degrade BP at 15 °C, were isolated from leaves and identified the DNA sequence of the CLE in one of the strains. Cutin was prepared from tomato leaves and treated with CLEs from 3 Cryptococcus species (C. magnus, Cryptococcus flavus, and Cryptococcus laurentii) and Pseudozyma antarctia (PaE). A typical cutin monomer, 10,16-dihydroxyhexadecanoic acid, was detected in extracts of the reaction solution via gas chromatography–mass spectrometry, showing that cutin was indeed degraded by CLEs. In addition to the aforementioned monomer, separation analysis via thin-layer chromatography detected high-molecular-weight products resulting from the breakdown of cutin by PaE, indicating that PaE acts as an endo-type enzyme. |
author2 |
Japan Society for the Promotion of Science Ministry of Education, Culture, Sports, Science and Technology Bio-oriented Technology Research Advancement Institution |
format |
Article in Journal/Newspaper |
author |
Ueda, Hirokazu Tabata, Jun Seshime, Yasuyo Masaki, Kazuo Sameshima-Yamashita, Yuka Kitamoto, Hiroko |
spellingShingle |
Ueda, Hirokazu Tabata, Jun Seshime, Yasuyo Masaki, Kazuo Sameshima-Yamashita, Yuka Kitamoto, Hiroko Cutinase-like biodegradable plastic-degrading enzymes from phylloplane yeasts have cutinase activity |
author_facet |
Ueda, Hirokazu Tabata, Jun Seshime, Yasuyo Masaki, Kazuo Sameshima-Yamashita, Yuka Kitamoto, Hiroko |
author_sort |
Ueda, Hirokazu |
title |
Cutinase-like biodegradable plastic-degrading enzymes from phylloplane yeasts have cutinase activity |
title_short |
Cutinase-like biodegradable plastic-degrading enzymes from phylloplane yeasts have cutinase activity |
title_full |
Cutinase-like biodegradable plastic-degrading enzymes from phylloplane yeasts have cutinase activity |
title_fullStr |
Cutinase-like biodegradable plastic-degrading enzymes from phylloplane yeasts have cutinase activity |
title_full_unstemmed |
Cutinase-like biodegradable plastic-degrading enzymes from phylloplane yeasts have cutinase activity |
title_sort |
cutinase-like biodegradable plastic-degrading enzymes from phylloplane yeasts have cutinase activity |
publisher |
Informa UK Limited |
publishDate |
2021 |
url |
http://dx.doi.org/10.1093/bbb/zbab113 http://academic.oup.com/bbb/advance-article-pdf/doi/10.1093/bbb/zbab113/38983601/zbab113.pdf http://academic.oup.com/bbb/article-pdf/85/8/1890/39278541/zbab113.pdf |
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Antarc* |
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Antarc* |
op_source |
Bioscience, Biotechnology, and Biochemistry volume 85, issue 8, page 1890-1898 ISSN 1347-6947 |
op_rights |
https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model |
op_doi |
https://doi.org/10.1093/bbb/zbab113 |
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Bioscience, Biotechnology, and Biochemistry |
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85 |
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8 |
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1890 |
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1898 |
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1810491625806233600 |