Structural and biophysical characterization of thermophilic enzymes prospected fro...
Full text | |
Author(s): |
Evangelista, Danilo Elton
[1]
;
Seiki Kadowaki, Marco Antonio
[1]
;
Mello, Bruno Luan
[1]
;
Polikarpov, Igor
[1]
Total Authors: 4
|
Affiliation: | [1] Univ Sao Paulo, Inst Fis Sao Carlos, Ave Trabalhador Sao Carlense 400, BR-13566590 Sao Carlos, SP - Brazil
Total Affiliations: 1
|
Document type: | Journal article |
Source: | International Journal of Biological Macromolecules; v. 109, p. 560-568, APR 2018. |
Web of Science Citations: | 4 |
Abstract | |
Environmental issues are promoting the development of innovative technologies for the production of renewable energy and ``green products{''} from plant biomass residues. These technologies rely on the conversion of the plant cell wall (PCW) polysaccharides into simple sugars, which involve synergistic activities of different PCW degrading enzymes, including xylanases; these are widely applied in food and feed sectors, paper and textile industries, among others. We cloned, expressed and biochemically characterized a novel xylanase (Xyn10) from the GH10 identified in a metatranscriptome of compost derived microbial consortia and determined its low-resolution SAXS molecular envelope in solution. Our results reveal that Xyn I 0 is a monomeric flexible globular enzyme, with high stability with a broad pH range from 4 to 10 and optimal activity conditions at pH 7 and 40 degrees C. Only 10% of activity loss was observed after the enzyme was incubated for 30 h at 40 degrees C with a pH ranging from 5 to 10. Moreover, Xyn10 maintained 100% of its initial activity after incubation for 120 h at 40 degrees C and 51% after incubation for 24 h at 50 degrees C (pH = 7.0). Xyn10 shows endocatalytic activity towards xylan and arabinoxylan, liberating xylose, xylobiose, 1,2-alpha-D-methylglucuronic acid decorated xylotriose, and 1,3-alpha-L-arabinofuranose decorated xylobiose and xylotriose oligosaccharides. (C) 2017 Elsevier B.V. All rights reserved. (AU) | |
FAPESP's process: | 15/13684-0 - Structural and functional studies of enzymes that participate in complex carbohydrates synthesis and degradation |
Grantee: | Igor Polikarpov |
Support type: | Research Projects - Thematic Grants |
FAPESP's process: | 11/20505-4 - Two important classes of glycosyl hydrolases: functional studies and structural analysis |
Grantee: | Marco Antonio Seiki Kadowaki |
Support type: | Scholarships in Brazil - Post-Doctorate |
FAPESP's process: | 10/52362-5 - Targeted analysis of microbial lignocellulolytic secretomes: a new approach to enzyme discovery |
Grantee: | Igor Polikarpov |
Support type: | Regular Research Grants |
FAPESP's process: | 11/21608-1 - Identification and characterization of new enzymes with potential for lignocellulosic biomass conversion |
Grantee: | Bruno Luan Soares Paula de Mello |
Support type: | Scholarships in Brazil - Doctorate (Direct) |