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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

A halotolerant bifunctional beta-xylosidase/alpha-L-arabinofuranosidase from Colletotrichum graminicola: Purification and biochemical characterization

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Author(s):
de Carvalho, Daniella Romano [1] ; Carli, Sibeli [1] ; Meleiro, Luana Parras [1] ; Rosa, Jose Cesar [2, 3] ; Cavalcante de Oliveira, Arthur Henrique [1] ; Jorge, Joao Atilio [4] ; Melo Furriel, Rosa Prazeres [1]
Total Authors: 7
Affiliation:
[1] Univ Sao Paulo, Fac Filosofia Ciencias & Letras Ribeirao Preto, Dept Quim, BR-14040901 Ribeirao Preto, SP - Brazil
[2] Univ Sao Paulo, Fac Med Ribeirao Preto, Ctr Quim Prot, BR-14049901 Ribeirao Preto - Brazil
[3] Univ Sao Paulo, Fac Med Ribeirao Preto, Dept Biol Celular & Mol & Bioagentes Patogen, BR-14049901 Ribeirao Preto - Brazil
[4] Univ Sao Paulo, Fac Filosofia Ciencias & Letras Ribeirao Preto, Dept Biol, BR-14040901 Ribeirao Preto, SP - Brazil
Total Affiliations: 4
Document type: Journal article
Source: International Journal of Biological Macromolecules; v. 114, p. 741-750, JUL 15 2018.
Web of Science Citations: 7
Abstract

A beta-xylosidase from Colletotrichum graminicola (Bxcg) was purified. The enzyme showed high halotolerance, retaining about 63% of the control activity in the presence of 2.5 mol L-1 NaCl. The presence of NaCI has not affected the optimum reaction temperature (65 degrees C), but the optimum pH was slightly altered (from 4.5 to 5.0) at high salt concentrations. Bxcg was fully stable at 50 degrees C for 24 h and over a wide pH range even in the presence of NaCI. In the absence of salt Bxcg hydrolyzed p-nitropheny1-beta-b-xylopyranoside with maximum velocity of 348.8 +/- 11.5 U mg(-1) and high catalytic efficiency (1432.7 +/- 47.3 L mmol(-1) s(-1). Bxcg revealed to be a bifunctional enzyme with both S-xylosidase and alpha-L-arabinofuranosidase activities, and hydrolyzed xylooligosaccharides containing up to six pentose residues. The enzyme showed high synergistic effect (3.1-fold) with an endo-xylanase for the hydrolysis of beechwood xylan, either in the absence or presence of 0.5 mol L-1 NaCI, and was tolerant to different organic solvents and surfactants. This is the first report of a halotolerant bifunctional beta-xylosidase/alpha-L-arabinofuranosidase from C graminicola, and the enzyme showed attractive properties for application in lignocellulose hydrolysis, particularly under high salinity and/or in the presence of residues of pretreatment steps. (C) 2018 Elsevier B.V. All rights reserved. (AU)

FAPESP's process: 17/13734-3 - Engineering of an endopolygalacturonase by insertion of different Carbohydrate Binding Modules (CBMs): chimerogenesis and proximity effects
Grantee:Sibeli de Carli
Support type: Scholarships in Brazil - Doctorate
FAPESP's process: 14/14415-0 - Lignocellulolytic enzymes from filamentous fungi: identification, purification, characterization, structure-function relationship and potential for biotechnological application
Grantee:Rosa dos Prazeres Melo Furriel
Support type: Regular Research Grants
FAPESP's process: 16/17582-0 - Thermostability modulation of a ß-glucosidase stimulated by glucose and xylose using site directed glycosylation
Grantee:Luana Parras Meleiro Garcia
Support type: Scholarships in Brazil - Post-Doctorate