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
| Autor: | Harald Kellner, René Ullrich, Do Huu Nghi, Marek J. Pecyna, Jussi Sipilä, Paula Nousiainen, Britta Bittner, Martin Hofrichter, Nico Jehmlich, Christiane Liers, Le Mai Huong |
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| Rok vydání: | 2012 |
| Předmět: |
Coumaric Acids
Glycoside Hydrolases Molecular Sequence Data Mycology Xylaria polymorpha Coumaric acid Lignin Applied Microbiology and Biotechnology Esterase Substrate Specificity 03 medical and health sciences Feruloyl esterase Hydrolase Glycoside hydrolase 030304 developmental biology chemistry.chemical_classification 0303 health sciences Xylariales Ecology biology 030306 microbiology Glycoside Sequence Analysis DNA 15. Life on land biology.organism_classification Hydroxycinnamic acid Wood Kinetics Biochemistry chemistry Carboxylic Ester Hydrolases Food Science Biotechnology |
| Zdroj: | Applied and Environmental Microbiology. 78:4893-4901 |
| ISSN: | 1098-5336 0099-2240 |
| Popis: | Soft rot (type II) fungi belonging to the family Xylariaceae are known to substantially degrade hardwood by means of their poorly understood lignocellulolytic system, which comprises various hydrolases, including feruloyl esterases and laccase. In the present study, several members of the Xylariaceae were found to exhibit high feruloyl esterase activity during growth on lignocellulosic materials such as wheat straw (up to 1,675 mU g −1 ) or beech wood (up to 80 mU g −1 ). Following the ester-cleaving activity toward methyl ferulate, a hydrolase of Xylaria polymorpha was produced in solid-state culture on wheat straw and purified by different steps of anion-exchange and size-exclusion chromatography to apparent homogeneity (specific activity, 2.2 U mg −1 ). The peptide sequence of the purified protein deduced from the gene sequence and verified by de novo peptide sequencing shows high similarity to putative α- l -rhamnosidase sequences belonging to the glycoside hydrolase family 78 (GH78; classified under EC 3.2.1.40). The purified enzyme (98 kDa by SDS-PAGE, 103 kDa by size-exclusion chromatography; pI 3.7) converted diverse glycosides (e.g., α- l -rhamnopyranoside and α- l -arabinofuranoside) but also natural and synthetic esters (e.g., chlorogenic acid, hydroxycinnamic acid glycoside esters, veratric acid esters, or p -nitrophenyl acetate) and released free hydroxycinnamic acids (ferulic and coumaric acid) from arabinoxylan and milled wheat straw. These catalytic properties strongly suggest that X. polymorpha GH78 is a multifunctional enzyme. It is the first fungal enzyme that combines glycosyl hydrolase with esterase activities and may help this soft rot fungus to degrade lignocelluloses. |
| Databáze: | OpenAIRE |
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