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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.)

Continuous production of xylooligosaccharides in a packed bed reactor with immobilized-stabilized biocatalysts of xylanase from Aspergillus versicolor

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Author(s):
Aragon, Caio C. [1, 2] ; Santos, Andrea F. [1] ; Ruiz-Matute, Ana I. [3] ; Corzo, Nieves [3] ; Guisan, Jose M. [2] ; Monti, Rubens [4] ; Mateo, Cesar [2]
Total Authors: 7
Affiliation:
[1] UNESP Univ Estadual Paulista, Dept Biochem & Chem Technol, Inst Chem, Araraquara, SP - Brazil
[2] CSIC, Inst Catalisis & Petroleoquim, E-28049 Madrid - Spain
[3] CSIC, Inst Invest Ciencias Alimentac CIAL, E-28049 Madrid - Spain
[4] UNESP Univ Estadual Paulista, Dept Food & Nutr, Fac Pharmaceut Sci, Araraquara, SP - Brazil
Total Affiliations: 4
Document type: Journal article
Source: JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC; v. 98, p. 8-14, DEC 30 2013.
Web of Science Citations: 14
Abstract

The production of xylooligosaccharides (XOS) using a packed-bed enzymatic reactor was studied at lab-scale. For this, a xylanase from Aspergillus versicolor was immobilized on different supports. The optimal derivative was xylanase immobilized on glyoxyl-agarose supports. This derivative preserved 85% of its catalytic activity; it was around 700-fold more stable than the soluble enzyme after incubation at 60 degrees C and was able to be reused for at least 101 h-cycles retaining full catalytic activity. About 18% of oligosaccharides with prebiotic interest (X2-X6) were produced by the glyoxyl derivative in batch hydrolysis. The production of xylobiose was 2.5-fold higher using the immobilized preparation than with soluble enzyme and small concentrations of xylose (<0.1%) were observed only at the end of the reaction. The derivative was employed on a packed bed reactor, and the continuous operation with no recirculation reached 56% and 70% of the end of reaction with flow rates of 60 mL/h and 12 mL/h, respectively. In continuous operation with recirculation at a flow rate of 60 mL/h, the reaction was completed after four hours. (C) 2013 Elsevier B.V. All rights reserved. (AU)

FAPESP's process: 08/09332-8 - Multipoint covalent immobilization of xylanases: selection of actives and stabilized derivatives
Grantee:Caio Casale Aragon
Support Opportunities: Scholarships in Brazil - Doctorate