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Multipoint covalent immobilization of xylanases: selection of actives and stabilized derivatives

Grant number: 08/09332-8
Support type:Scholarships in Brazil - Doctorate
Effective date (Start): May 01, 2009
Effective date (End): February 28, 2013
Field of knowledge:Biological Sciences - Biochemistry - Enzymology
Principal researcher:Rubens Monti
Grantee:Caio Casale Aragon
Home Institution: Instituto de Química (IQ). Universidade Estadual Paulista (UNESP). Campus de Araraquara. Araraquara , SP, Brazil

Abstract

Xylanases (EC 3.2.1.8; endo-1,4-b-xylanase) and xylosidases (EC 3.2.1.37; xylan 1,4-b-xylosidase) are glycosidases that catalyze, respectively, the hydrolysis of the 1,4-b-xylosidic linkages of xylans and the hydrolysis of xylooligosaccharides and xylobiose, producing xylose. The xylan-degrading enzymes of several microorganisms have been extensively studied during the last decade, because of their importance in many industrial processes, for example, in clarification of juices and wines, bread manufacture, xylose and xylitol productions; they are also used in the beer, animal feed, paper and cellulose industries. Although they have plenty of applications, these enzymes have not all their potential explored. Their immobilization on solid supports offers a lot of advantages, including the reuse of the enzyme, the easy separation of the product, and the increase of enzymatic stability. The objectives of this work are: a) to produce the thermophilics enzymes xylanase and xylosidase, by using a fungi isolated in the laboratory (FCUP1), besides Humicola grisea var. thermoidea and Aspergillus versicolor; b) to accomplish multipoint covalent immobilization of thermophilics xilanases and xylosidases of filamentous fungi in solid supports, with kinetic characterization of those more actives and stabilized derivatives, comparing them with the free enzymes; c) to accomplish the hydrolysis of xylan using, concomitantly, xylanase and xylosidase derivatives; d) to evaluate the reuse capacity of the actives and stabilized derivatives. Immobilization studies of thermostable xylan-degrading enzymes are scarce, but fundamental to optimization and cost reduction in the many applications.

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Scientific publications
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
ARAGON, CAIO C.; SANTOS, ANDREA F.; RUIZ-MATUTE, ANA I.; CORZO, NIEVES; GUISAN, JOSE M.; MONTI, RUBENS; MATEO, CESAR. Continuous production of xylooligosaccharides in a packed bed reactor with immobilized-stabilized biocatalysts of xylanase from Aspergillus versicolor. JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, v. 98, p. 8-14, DEC 30 2013. Web of Science Citations: 14.
ARAGON, CAIO C.; MATEO, CESAR; RUIZ-MATUTE, ANA I.; CORZO, NIEVES; FERNANDEZ-LORENTE, GLORIA; SEVILLANO, LAURA; DIAZ, MARGARITA; MONTI, RUBENS; SANTAMARIA, RAMON I.; GUISAN, JOSE M. Production of xylo-oligosaccharides by immobilized-stabilized derivatives of endo-xylanase from Streptomyces halstedii. Process Biochemistry, v. 48, n. 3, p. 478-483, MAR 2013. Web of Science Citations: 24.

Please report errors in scientific publications list by writing to: cdi@fapesp.br.