Production of CGTase by a bacillus Alkalophilic CGII strain isolated from wastewater of a manioc flour industry

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorFreitas, Telma Luisa de
dc.creatorMonti, Rubens
dc.creatorContiero, Jonas
dc.date2014-05-27T11:21:12Z
dc.date2016-10-25T18:20:09Z
dc.date2014-05-27T11:21:12Z
dc.date2016-10-25T18:20:09Z
dc.date2004-12-01
dc.date.accessioned2017-04-06T01:11:14Z
dc.date.available2017-04-06T01:11:14Z
dc.identifierBrazilian Journal of Microbiology, v. 35, n. 3, p. 255-260, 2004.
dc.identifier1517-8382
dc.identifierhttp://hdl.handle.net/11449/67995
dc.identifierhttp://acervodigital.unesp.br/handle/11449/67995
dc.identifier10.1590/S1517-83822004000200015
dc.identifierS1517-83822004000200015
dc.identifierWOS:000234802600015
dc.identifier2-s2.0-19944363225.pdf
dc.identifier2-s2.0-19944363225
dc.identifierhttp://dx.doi.org/10.1590/S1517-83822004000200015
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/889378
dc.descriptionGCTase production by a new strain of Bacillus alkalophillc CGII isolated from Brazilian wastewater of manioc flour industry was examined. The growth medium used was composed by 1.5% starch, 1.5% nitrogen and 1% Na 2CO3. Higher activity was obtained with starch, maltodextrin and galactose. When glucose was added to the medium, no enzyme production was observed. High enzyme activity and growth were reached when aeration was increased (88.6 U/mL). The enzyme characterization showed an optimum pH and temperature 8.0 and 55°C for starch hydrolyses, respectively. Mg+ and Ca++ showed small activation; however, Hg + and Cu+ showed a strong enzyme inhibition.
dc.languageeng
dc.relationBrazilian Journal of Microbiology
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectβ-cyclodextrin
dc.subjectBacillus alkalophilic CGII
dc.subjectCGTase
dc.subjectEnzyme activity
dc.subjectStarch hydrolysis
dc.subjectManihot esculenta
dc.titleProduction of CGTase by a bacillus Alkalophilic CGII strain isolated from wastewater of a manioc flour industry
dc.typeOtro


Este ítem pertenece a la siguiente institución