Factors influencing β-glucosidase production, activity and stability in Nectria catalinensis

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The influence of different cultivation conditions on β-glucosidase production and of some parameters on the activity and stability of this enzyme were studied in Nectria catalinensis. Maximal β-glucosidase production was achieved with ammonium nitrate (0.5 g N/L) as nitrogen source. Tween 80, Tween...

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Detalles Bibliográficos
Autor principal: Pardo, A.G
Otros Autores: Forchiassin, F.
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: Czech Academy of Sciences 1999
Acceso en línea:Registro en Scopus
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Biblioteca Central Dr. Luis F. Leloir (FCEN) de Universidad de Buenos Aires
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030 |a FOMIA 
100 1 |a Pardo, A.G. 
245 1 0 |a Factors influencing β-glucosidase production, activity and stability in Nectria catalinensis 
260 |b Czech Academy of Sciences  |c 1999 
270 1 0 |m Forchiassin, F.; Lab. de Micología Exp., Depto. de Ciencias Biológicas, Universidad de Buenos Aires, 1428 - Buenos Aires, Argentina; email: fla@bg.fcen.uba.ar 
506 |2 openaire  |e Política editorial 
504 |a Bradford, M.M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein-dye binding (1976) Anal.Biochem., 72, pp. 248-254 
504 |a Brown, J.A., Falconer, D.J., Wood, T.M., Isolation and properties of mutants of the fungus Penicillium pinophilum with enhanced cellulase and β-glucosidase production (1987) Enzyme Microb. Technol., 9, pp. 169-175 
504 |a Dekker, R.F.H., Kinetics, inhibition and stability properties of a commercial β-glucosidase (cellobiase) preparation from Aspergillus niger and its suitability in the hydrolysis of lignocellulose (1986) Biotechnol.bioeng., 28, pp. 1438-1442 
504 |a Eriksson, K.E., Enzyme mechanism involved in cellulose hydrolysis by the rot fungus Sporotrichum pulverulentum (1978) Biotechnol. Bioeng., 20, pp. 317-332 
504 |a Hulme, M.A., Stranks, D.W., Induction and regulation of production of cellulase by fungi (1970) Nature, 226, pp. 469-470 
504 |a Jackson, M.A., Talburt, D.E., Mechanism for β-glucosidase release into cellulose-growth Trichoderma reesei culture supernatant (1988) Exp.Mycol., 12, pp. 203-216 
504 |a Lima, C.E., Forchiassin, F., Ranalli, M.E., Systematic and biological study of Hypocreales of Argentina. IV. Nectria catalinensis sp.nov (1988) Nova Hedwigia, 46, pp. 149-156 
504 |a Magnelli, P.E., Ramos, A., Forchiassin, F., Factors influencing β-glucosidase production in Saccobolus saccoboloides (1996) Mycologia, 88, pp. 249-255 
504 |a Messner, R., Hagspiel, K., Kubicek, C.P., Isolation of a β-glucosidase binding and activating polysaccharide from cell walls of Trichoderma reesei (1990) Arch.Microbiol., 154, pp. 150-155 
504 |a Montgomery, R.A.P., The role of polysaccharidase enzymes in the decay of wood by Basidimycetes (1982) Decomposer Basidiomycetes: Their Biology and Ecology, pp. 51-56. , J.C. Frankland, J.N. Hedger, M.J. Swift (Eds): Cambridge University Press, Cambridge 
504 |a Oguntimein, G.B., Moo-Young, M., Production and properties of β-glucosidase by Neurospora sitophila (1991) World J.Microbiol.Biotechnol., 7, pp. 4-11 
504 |a Pardo, A.G., Effect of surfactants on cellulase production by Nectria catalinensis (1996) Curr.Microbiol., 33, pp. 275-278 
504 |a Pardo, A.G., Forchiassin, F., Inducción-represión de la actividad celulolítica en Nectria catalinensis (Ascomycotina) (1994) Bol.Soc. Argent.Bot., 30, pp. 43-49 
504 |a Pardo, A.G., Forchiassin, F., Efecto de cationes sobre la producción y actividad del sistema celulasa de Nectria catalinensis (Fungi, Ascomycetes) (1995) Bol.Soc.Argent.Bot., 30, pp. 137-148 
504 |a Pardo, A.G., Sívori, A.S., Ranalli, M.E., Comparative study of cellulolytic enzyme zymograms of species of Thecotheus and lodophanus (Pezizales-Ascomycetes) (1997) Mycotaxon, 63, pp. 269-286 
504 |a Reese, E.T., Lola, J.E., Parrish, F.W., Modified substrates and modified products as inducers of carbohydrases (1969) J.Bacteriol., 100, pp. 1151-1154 
504 |a Reese, E.T., Manguire, A., Surfactants as stimulants of enzyme production by microorganisms (1969) Appl.Microbiol., 17, pp. 242-245 
504 |a Workman, W.E., Day, D.F., Purification and properties of β-glucosidase from Aspergillus terreus (1982) Appl.Environ.Microbiol., 44, pp. 1289-1295 
504 |a Ximenes, E.A., Felix, C.R., Ulhoa, C.J., Production of cellulases by Aspergillus fumigatus and characterisation of one β-glucosidase (1996) Curr.Microbiol., 32, pp. 119-123 
504 |a Ximenes, E.A., Filho, E.X.F., Purification and characterization of a β-glucosidase from solid-state cultures of Humicola grisea var. thermoidea (1996) Can.J.Microbiol., 42, pp. 1-5 
504 |a Yazdi, T., Woodward, J.R., Radford, A., Cellulase production by Neurospora crassa: Induction and optimisation of the enzyme complex (1990) Enzyme Microb.Technol., 12, pp. 116-119 
504 |a Yazdi, T., Woodward, J.R., Radford, A., The cellulase complex of Neurospora crassa: Activity, stability and release (1990) J.Gen. Microbiol., 136, pp. 1313-1319 
520 3 |a The influence of different cultivation conditions on β-glucosidase production and of some parameters on the activity and stability of this enzyme were studied in Nectria catalinensis. Maximal β-glucosidase production was achieved with ammonium nitrate (0.5 g N/L) as nitrogen source. Tween 80, Tween 20 and Triton X-100 increased β-glucosidase yields, Tween 80 was the most effective for enzyme release and growth at a concentration of 3.4 mmol/L. On the other hand, Tween 20 and Triton X-100 had an inhibitory effect on N. catalinensis growth. A temperature of 23 °C and an initial pH of cultures of 6.5 were optimal for biomass and β-glucosidase production. Under optimal cultural conditions (ammonium nitrate, 0.5 g N/L; Tween 80, 3.4 mmol/L; 23 °C; initial pH 6.5) the β-glucosidase yield was increased more than five fold respect to the initial state. Optimal temperature for β-glucosidase activity was 45 °C, the initial activity dropped 60 % after 6 h of incubation at this temperature. Optimal PH for enzyme activity was 5.3. At this pH the β-glucosidase was completely stable after 3 d of incubation The V and Km values calculated from Lineweaver-Burk and Eadie-Hofstee plots were 0.23 μmol 4-nitrophenol per min per mg of protein and 0.25 mmol 4-nitrophenol β-D-glucopyranoside per L, respectively. The activation energy according to Arrhenius plot was 49.6 KJ/mol.  |l eng 
536 |a Detalles de la financiación: Universidad de Buenos Aires 
536 |a Detalles de la financiación: The authors acknowledge CONICET de Buenos Aires for financial support. 
593 |a Lab. de Micología Exp., Depto. de Ciencias Biológicas, Universidad de Buenos Aires, 1428 - Buenos Aires, Argentina 
593 |a U. de Invest. en Interacciones Biol., Centro de Estudios e Investigations, Universidad Nacional de Quilmes, 1876 - Provincia de Buenos Aires, Argentina 
690 1 0 |a ARRHENIUS 
700 1 |a Forchiassin, F. 
773 0 |d Czech Academy of Sciences, 1999  |g v. 44  |h pp. 71-76  |k n. 1  |p Folia Microbiol.  |x 00155632  |t Folia Microbiologica 
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856 4 0 |u https://doi.org/10.1007/BF02816225  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_00155632_v44_n1_p71_Pardo  |y Handle 
856 4 0 |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00155632_v44_n1_p71_Pardo  |y Registro en la Biblioteca Digital 
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