dc.creatorAquino Neto, Sidney
dc.creatorForti, Juliane C.
dc.creatorZucolotto, Valtencir
dc.creatorCiancaglini, Pietro
dc.creatorAndrade, Adalgisa Rodrigues de
dc.date.accessioned2016-04-25T14:04:02Z
dc.date.accessioned2018-07-04T16:53:48Z
dc.date.available2016-04-25T14:04:02Z
dc.date.available2018-07-04T16:53:48Z
dc.date.created2016-04-25T14:04:02Z
dc.date.issued2011-12
dc.identifierProcess Biochemistry, Oxford : Elsevier, v. 46, n. 12, p. 2347-2352, Dec. 2011
dc.identifier1359-5113
dc.identifierhttp://www.producao.usp.br/handle/BDPI/50097
dc.identifier10.1016/j.procbio.2011.09.019
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1641846
dc.description.abstractThis paper describes the kinetic behavior of alcohol (ADH) and aldehyde (AldDH) dehydrogenases in solution and immobilized onto carbon platform via polyamidoamine (PAMAM) dendrimers. All the kinetic constants achieved for soluble ADH and AldDH are in agreement with literature data. The influence of pH and temperature was evaluated. Results showed that physiological conditions and ambient temperature can satisfactorily be applied to systems containing dehydrogenase enzymes, so as to ensure an environment where both ADH and AldDH display good activity. It is noteworthy that the affinity between both ADH and AldDH and their substrates and coenzyme is retained after the immobilization process. Investigation of the influence of the storage time demonstrated that there was no appreciable reduction in enzymatic activity for 50 days. Results showed that the PAMAM dendrimers provide a good environment for immobilization of dehydrogenase enzymes and that the affinity observed between the enzymes and their substrates and coenzymes seems to be retained, despite the considerable loss of enzymatic activity after immobilization. Furthermore, the anchoring methodology employed herein, namely layer-by-layer (LbL), required very low catalyst consumption.
dc.languageeng
dc.publisherElsevier
dc.publisherOxford
dc.relationProcess Biochemistry
dc.rightsCopyright Elsevier Ltd.
dc.rightsrestrictedAccess
dc.subjectAlcohol dehydrogenase
dc.subjectAldehyde dehydrogenase
dc.subjectPAMAM
dc.subjectEnzyme immobilization
dc.titleThe kinetic behavior of dehydrogenase enzymes in solution and immobilized onto nanostructured carbon platforms
dc.typeArtículos de revistas


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