dc.contributor | Universidade Estadual Paulista (UNESP) | |
dc.creator | Azevedo Carvalho, Ana Flávia | |
dc.creator | Zorzetto Gonçalves, Aline | |
dc.creator | Da Silva, Roberto | |
dc.creator | Gomes, Eleni | |
dc.date | 2014-05-27T11:22:21Z | |
dc.date | 2016-10-25T18:23:23Z | |
dc.date | 2014-05-27T11:22:21Z | |
dc.date | 2016-10-25T18:23:23Z | |
dc.date | 2006-12-13 | |
dc.date.accessioned | 2017-04-06T01:23:04Z | |
dc.date.available | 2017-04-06T01:23:04Z | |
dc.identifier | Journal of Microbiology, v. 44, n. 3, p. 276-283, 2006. | |
dc.identifier | 1225-8873 | |
dc.identifier | http://hdl.handle.net/11449/69425 | |
dc.identifier | http://acervodigital.unesp.br/handle/11449/69425 | |
dc.identifier | WOS:000238780500004 | |
dc.identifier | 2-s2.0-33747823854.pdf | |
dc.identifier | 2-s2.0-33747823854 | |
dc.identifier | http://www.ncbi.nlm.nih.gov/pubmed/16820757 | |
dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/890676 | |
dc.description | The thermophilic fungus Thermoascus aurantiacus 179-5 produced large quantities of a glucosidase which preferentially hydrolyzed maltose over starch. Enzyme production was high in submerged fermentation, with a maximal activity of 30 U/ml after 336 h of fermentation. In solid-state fermentation, the activity of the enzyme was 22 U/ml at 144 h in medium containing wheat bran and 5.8 U/ml at 48 h when cassava pulp was used as the culture medium. The enzyme was specific for maltose, very slowly hydrolyzed starch, dextrins (2-7G) and the synthetic substrate (α-PNPG), and did not hydrolyze sucrose. These properties suggest that the enzyme is a type II α-glucosidase. The optimum temperature of the enzyme was 70°C. In addition, the enzyme was highly thermostable (100% stability for 10 h at 60°C and a half-life of 15 min at 80°C), and stable within a wide pH range. Copyright © 2006, The Microbiological Society of Korea. | |
dc.language | eng | |
dc.relation | Journal of Microbiology | |
dc.rights | info:eu-repo/semantics/openAccess | |
dc.subject | Glucosidase | |
dc.subject | Solid-state fermentation | |
dc.subject | Submerged fermentation | |
dc.subject | Thermoascus | |
dc.subject | Thermophilic | |
dc.subject | Thermostable | |
dc.subject | Fungi | |
dc.subject | Manihot esculenta | |
dc.subject | Thermoascus aurantiacus | |
dc.subject | Triticum aestivum | |
dc.subject | dextrin | |
dc.subject | glucosidase | |
dc.subject | culture medium | |
dc.subject | enzyme specificity | |
dc.subject | enzyme stability | |
dc.subject | enzymology | |
dc.subject | Eurotiales | |
dc.subject | fermentation | |
dc.subject | growth, development and aging | |
dc.subject | heat | |
dc.subject | hydrolysis | |
dc.subject | metabolism | |
dc.subject | pH | |
dc.subject | Culture Media | |
dc.subject | Dextrins | |
dc.subject | Enzyme Stability | |
dc.subject | Fermentation | |
dc.subject | Glucosidases | |
dc.subject | Heat | |
dc.subject | Hydrogen-Ion Concentration | |
dc.subject | Hydrolysis | |
dc.subject | Substrate Specificity | |
dc.title | A specific short dextrin-hydrolyzing extracellular glucosidase from the thermophilic fungus Thermoascus aurantiacus 179-5 | |
dc.type | Otro | |