Purification of an exopolygalacturonase from Penicillium viridicatum RFC3 produced in submerged fermentation

dc.contributorUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-27T11:24:04Z
dc.date.accessioned2022-10-05T18:18:40Z
dc.date.available2014-05-27T11:24:04Z
dc.date.available2022-10-05T18:18:40Z
dc.date.created2014-05-27T11:24:04Z
dc.date.issued2009-12-01
dc.identifierInternational Journal of Microbiology.
dc.identifier1687-918X
dc.identifier1687-9198
dc.identifierhttp://hdl.handle.net/11449/71313
dc.identifier10.1155/2009/631942
dc.identifier2-s2.0-80052506411
dc.identifier2-s2.0-80052506411.pdf
dc.identifier7091241742851920
dc.identifier9424175688206545
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/3920511
dc.description.abstractAn exo-PG obtained from Penicillium viridicatum in submerged fermentation was purified to homogeneity. The apparent molecular weight of the enzyme was 92 kDa, optimum pH and temperature for activity were pH 5 and 50-55°C. The exo-PG showed a profile of an exo-polygalacturonase, releasing galacturonic acid by hydrolysis of pectin with a high degree of esterification (D.E.). Ions Ca 2+ enhanced the stability of enzyme and its activity by 30%. The K m was 1.30 in absence of Ca 2+ and 1.16mg mL -1 in presence of this ion. In relation to the Vmax the presence of this ion increased from 1.76 to 2.07 μmol min -1mg -1. Copyright © 2009 Eleni Gomes et al.
dc.languageeng
dc.relationInternational Journal of Microbiology
dc.relation0,662
dc.rightsAcesso aberto
dc.sourceScopus
dc.subjectPenicillium
dc.subjectPenicillium viridicatum
dc.titlePurification of an exopolygalacturonase from Penicillium viridicatum RFC3 produced in submerged fermentation
dc.typeArtigo


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