Unwrapping the hydrolytic system of the phytopathogenic fungus Phoma exigua by secretome analysis |
| |
| Institution: | 1. Division of Microbiology, Indian Agricultural Research Institute, New Delhi 110012, India;2. Central Instrumentation Facility, Biotech Center, University of Delhi South Campus, New Delhi 110021, India;1. Food Research Department, School of Chemistry, Universidad Autónoma de Coahuila, Saltillo 25280, Coahuila, Mexico;2. Department of Biotechnology, Universidad Autónoma Metropolitana Iztapalapa, 09340 México, D.F., Mexico;3. Animal Nutrition Department, Universidad Autónoma Agraria Antonio Narro, Saltillo 25315, Coahuila, Mexico;1. Department of Chemistry, Wroclaw University of Environmental and Life Sciences, Norwida 25, 50-375 Wrocław, Poland;2. Department of Special Analyses, Research and Teaching Institute for Brewing (VLB – Berlin e.V.), Seestr. 13, D-13353 Berlin, Germany;1. College of Biological and Environmental Sciences, Zhejiang Wanli University, Ningbo 315100, PR China;2. Molecular Inflammation Research Center for Aging Intervention (MRCA), College of Pharmacy, Pusan National University, Busan 609-735, South Korea;3. Zhejiang Provincial Key Laboratory of Applied Enzymology, Yangtze Delta Region Institute of Tsinghua University, Jiaxing 314006, PR China;4. Department of Dermatology, Sungkyunkwan University School of Medicine, Samsung Medical Center, Seoul 135-710, South Korea;1. School of Life Sciences and Chemical Technology, Ngee Ann Polytechnic, Singapore;2. State Key Laboratory of Microbial Metabolism, and Laboratory of Molecular Biochemical Engineering, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, China |
| |
| Abstract: | The present work describes the secretome profiling of a phytopathogenic fungus, Phoma exigua by liquid chromatography coupled tandem mass spectrometry (LC–MS/MS) based proteomics approach to highlight the suites of enzymes responsible for biomass hydrolysis. Mass spectrometry identified 33 proteins in the Phoma secretome when grown on α-cellulose as the sole carbon source. The functional classification revealed a unique extracellular enzyme system mainly belonging to the family of glycosyl hydrolase proteins (52%). This hydrolytic system consisted of cellulases (endo-1,4-β-glucanase, cellobiohydrolase I, exoglucanase, and β-glucosidase), hemicellulases (1,4-β-xylosidase and endo-1,4-β-xylanase) and other hypothetical proteins including GH3, GH5, GH6, GH7, GH11, GH20, GH32 and GH54. The synergistic action of this enzyme cocktail was assessed by the saccharification of alkali treated wheat straw. Since the Phoma secretome has limited β-glucosidase activity, it was supplemented with commercial β-glucosidase. After supplementation, this enzyme complex resulted in high yields of glucose (177.2 ± 1.0 mg/gds), xylose (209.2 ± 1.5 mg/gds) and arabinose (25.2 ± 0.3 mg/gds). The secretome analysis and biomass hydrolysis by P. exigua revealed its unique potential as a source of hydrolytic enzymes for lignocellulosic biomass hydrolysis. |
| |
| Keywords: | Secretome Glycosyl hydrolase Biomass hydrolysis |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
