Comprehensive Analysis of Carbohydrate-Active Enzymes from the Filamentous Fungus Scytalidium candidum 3C
- Авторы: Pavlov I.1, Eneyskaya E.1, Bobrov K.1, Polev D.2, Ivanen D.1, Kopylov A.3, Naryzhny S.1,3, Kulminskaya A.1,4
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Учреждения:
- National Research Center “Kurchatov Institute”
- Resource Center for Molecular and Cell Technologies and “Centre Biobank”
- Orekhovich Institute of Biomedical Chemistry
- Department of Medical Physics
- Выпуск: Том 83, № 11 (2018)
- Страницы: 1399-1410
- Раздел: Article
- URL: https://journals.rcsi.science/0006-2979/article/view/151761
- DOI: https://doi.org/10.1134/S000629791811010X
- ID: 151761
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Аннотация
Complete enzymatic degradation of plant polysaccharides is a result of combined action of various carbohydrate-active enzymes (CAZymes). In this paper, we demonstrate the potential of the filamentous fungus Scytalidium candidum 3C for processing of plant biomass. Structural annotation of the improved assembly of S. candidum 3C genome and functional annotation of CAZymes revealed putative gene sequences encoding such proteins. A total of 190 CAZyme-encoding genes were identified, including 104 glycoside hydrolases, 52 glycosyltransferases, 28 oxidative enzymes, and 6 carbohydrate esterases. In addition, 14 carbohydrate-binding modules were found. Glycoside hydrolases secreted during the growth of S. candidum 3C in three media were analyzed with a variety of substrates. Mass spectrometry analysis of the fungal culture liquid revealed the presence of peptides identical to 36 glycoside hydrolases, three proteins without known enzymatic function belonging to the same group of families, and 11 oxidative enzymes. The activity of endohemicellulases was determined using specially synthesized substrates in which the glycosidic bond between monosaccharide residues was replaced by a thiolinkage. During analysis of the CAZyme profile of S. candidum 3C, four β-xylanases from the GH10 family and two β-glucanases from the GH7 and GH55 families were detected, partially purified, and identified.
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Об авторах
I. Pavlov
National Research Center “Kurchatov Institute”
Email: kulminskaya_aa@pnpi.nrcki.ru
Россия, Gatchina, Leningrad Region, 188300
E. Eneyskaya
National Research Center “Kurchatov Institute”
Email: kulminskaya_aa@pnpi.nrcki.ru
Россия, Gatchina, Leningrad Region, 188300
K. Bobrov
National Research Center “Kurchatov Institute”
Email: kulminskaya_aa@pnpi.nrcki.ru
Россия, Gatchina, Leningrad Region, 188300
D. Polev
Resource Center for Molecular and Cell Technologies and “Centre Biobank”
Email: kulminskaya_aa@pnpi.nrcki.ru
Россия, St. Petersburg, 198504
D. Ivanen
National Research Center “Kurchatov Institute”
Email: kulminskaya_aa@pnpi.nrcki.ru
Россия, Gatchina, Leningrad Region, 188300
A. Kopylov
Orekhovich Institute of Biomedical Chemistry
Email: kulminskaya_aa@pnpi.nrcki.ru
Россия, Moscow, 119121
S. Naryzhny
National Research Center “Kurchatov Institute”; Orekhovich Institute of Biomedical Chemistry
Email: kulminskaya_aa@pnpi.nrcki.ru
Россия, Gatchina, Leningrad Region, 188300; Moscow, 119121
A. Kulminskaya
National Research Center “Kurchatov Institute”; Department of Medical Physics
Автор, ответственный за переписку.
Email: kulminskaya_aa@pnpi.nrcki.ru
Россия, Gatchina, Leningrad Region, 188300; St. Petersburg, 194021