dc.contributorUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T14:02:57Z
dc.date.available2014-05-20T14:02:57Z
dc.date.created2014-05-20T14:02:57Z
dc.date.issued2007-01-01
dc.identifierFood Chemistry. Oxford: Elsevier B.V., v. 104, n. 1, p. 127-131, 2007.
dc.identifier0308-8146
dc.identifierhttp://hdl.handle.net/11449/22180
dc.identifier10.1016/j.foodchem.2006.11.010
dc.identifierWOS:000246630500018
dc.identifier7091241742851920
dc.identifier9424175688206545
dc.identifier0000-0003-0935-1387
dc.description.abstractProteases are one of the most important groups of industrial enzymes, with considerable application in the food industry. The aim of this work was to study a novel protease produced by the thermophilic fungus, Thermoascus aurantiacus, through solid-state fermentation (SSF). The enzyme acted optimally at pH 5.5 and 60 degrees C it was stable up to 60 degrees C for 1 h and in the pH range 3.0-9.5. To elucidate the enzyme's proteolytic activity, its hydrolytic profile on bovine casein, an important protein in the food industry, was studied by enzymatic hydrolysis on skim milk, analyzed by gel electrophoresis (UREA-PAGE), which clearly showed that the protease does not have the same specificity as bovine chymosin. (c) 2006 Elsevier Ltd. All rights reserved.
dc.languageeng
dc.publisherElsevier B.V.
dc.relationFood Chemistry
dc.relation4.946
dc.relation1,793
dc.rightsAcesso restrito
dc.sourceWeb of Science
dc.subjectSSF
dc.subjectprotease
dc.subjectwheat bran
dc.subjectcasein
dc.subjectproteolytic activity
dc.subjectcharacterization
dc.subjectHydrolysis
dc.subjectelectrophoresis
dc.titlePartial characterization of protease from a thermophilic fungus, Thermoascus aurantiacus, and its hydrolytic activity on bovine casein
dc.typeArtículos de revistas


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