Beta-glucosidase activity of a thermophilic cellulolytic fungus, Humicola sp.
| dc.contributor.author | Araujo, E. F. | |
| dc.contributor.author | Barros, E. G. | |
| dc.contributor.author | Caldas, R. A. | |
| dc.contributor.author | Silva, D. O. | |
| dc.date.accessioned | 2019-01-07T14:37:04Z | |
| dc.date.available | 2019-01-07T14:37:04Z | |
| dc.date.issued | 1983-11 | |
| dc.description.abstract | The beta-glucosidase of aHumicola sp. is partly characterized. The pH and temperature optima, thermal stability and Michaelis constants with p-nitrophenyl-beta-D-glucoside (PNPG) substrate suggest the existance of at least one extracellular and one intracellular enzyme. The extracellular activity is substantially more than that produced byTrichoderma reesei QM 9414. | en |
| dc.format | pt-BR | |
| dc.identifier.issn | 1573-6776 | |
| dc.identifier.uri | https://doi.org/10.1007/BF01386502 | |
| dc.identifier.uri | http://www.locus.ufv.br/handle/123456789/22925 | |
| dc.language.iso | eng | pt-BR |
| dc.publisher | Biotechnology Letters | pt-BR |
| dc.relation.ispartofseries | Volume 5, Issue 11, p. 781–784, November 1983 | pt-BR |
| dc.rights | Kluwer Academic Publishers | pt-BR |
| dc.subject | Enzyme | pt-BR |
| dc.subject | Thermal stability | pt-BR |
| dc.subject | Intracellular enzyme | pt-BR |
| dc.subject | Humicola | pt-BR |
| dc.subject | Extracellular activity | pt-BR |
| dc.title | Beta-glucosidase activity of a thermophilic cellulolytic fungus, Humicola sp. | en |
| dc.type | Artigo | pt-BR |
