Advanced search
Start date

Development of beta-glycosidases designed to improve the efficiency of noncomplexed cellulase systems


The rate of the enzymatic hydrolysis of cellulose decreases along the reaction time, which represents a drawback for the productivity of this process. One of the factors causing that problem is the cellobiose inhibitory action upon the “cellulases” (endoglucanases and cellobiohydrolases) that catalyze the hydrolysis. This project aims to stabilize the rate of the enzymatic hydrolysis of cellulose by developing β-glycosidases designed to reduce the cellobiose inhibitory effect on the “cellulases”. Such development will be based on the β-glycosidase (cellobiase) from the fall armyworm Spodoptera frugiperda (Sfβgly) and the “carbohydrate binding domain” of the endoglucanase EngXCA from Xhantomonas axonopodis pv citri (CBMXAC). Firstly, a chimeric protein resulting from the fusion of Sfβgly and CBMXAC will be assembled. The targeting of Sfβgly to the surface of the cellulose fibers (due the presence of a CBM) could decrease the cellobiose concentration directly in the microenvironment of action of the endoglucanases and cellobiohydrolases. Thus the action of Sfβgly-CBM could reduce the cellobiose inhibitory effect and sustain a high activity of endoglucanases and cellobiohydrolases for a longer time. This project also intends to improve the participation of the β-glycosidases in the cellulose hydrolysis by selecting mutant Sfβgly that presents high hydrolytic activity upon cellobiose. Libraries of random mutant Sfβgly will be generated and screened based on the ratio of activity upon cellobiose versus synthetic substrates. Finally, amino acid residues networks involved in the determination of Sfβgly substrate specificity and catalytic activity will be identified by using structural analysis, site-directed mutagenesis studies and enzyme kinetic experiments. (AU)

Articles published in Agência FAPESP Newsletter about the research grant:
Articles published in other media outlets (0 total):
More itemsLess items

Scientific publications (7)
(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)
TAMAKI, FABIO K.; SOUZA, DIORGE P.; SOUZA, VALQUIRIA P.; IKEGAMI, CECILIA M.; FARAH, CHUCK S.; MARANA, SANDRO R.. Using the Amino Acid Network to Modulate the Hydrolytic Activity of beta-Glycosidases. PLoS One, v. 11, n. 12, . (08/55914-9, 14/19439-5)
SAYEGH, RAPHAEL S. R.; TAMAKI, FABIO K.; MARANA, SANDRO R.; SALINAS, ROBERTO K.; ARANTES, GUILHERME M.. Conformational flexibility of the complete catalytic domain of Cdc25B phosphatases. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, v. 84, n. 11, p. 1567-1575, . (14/19439-5, 08/55914-9, 13/17883-2, 14/21900-2, 12/00543-1)
BETON, DANIELA; MARANA, SANDRO R.. Half-Barrels Derived from a (beta/alpha)(8) Barrel beta-Glycosidase Undergo an Activation Process. PLoS One, v. 10, n. 10, . (08/55914-9)
FRUTUOSO, M. A.; MARANA, S. R.. A Single Amino Acid Residue Determines the Ratio of Hydrolysis to Transglycosylation Catalyzed by beta-Glucosidases. PROTEIN AND PEPTIDE LETTERS, v. 20, n. 1, p. 102-106, . (08/55914-9)
MENDONCA, LUCIO M. F.; MARANA, SANDRO R.. Single mutations outside the active site affect the substrate specificity in a beta-glycosidase. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, v. 1814, n. 12, p. 1616-1623, . (08/55914-9)
SOUZA, VALQUIRIA P.; IKEGAMI, CECILIA M.; ARANTES, GUILHERME M.; MARANA, SANDRO R.. Protein thermal denaturation is modulated by central residues in the protein structure network. FEBS Journal, v. 283, n. 6, p. 1124-1138, . (14/21900-2, 08/55914-9, 14/19439-5)
GONCALVES, LARISSA M.; CHAIMOVICH, HERNAN; CUCCOVIA, IOLANDA M.; MARANA, SANDRO R.. Chimeric Proteins Combining Phosphatase and Cellulose-Binding Activities: Proof-of-Concept and Application in the Hydrolysis of Paraoxon. PROTEIN AND PEPTIDE LETTERS, v. 21, n. 5, p. 468-475, . (08/55914-9)

Please report errors in scientific publications list by writing to: