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Investigation of structural effects and behaviour of pseudomonas aeruginosa amidase encapsulated in reserved micelles

2012-02Journal article Restricted access
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dc.contributor.authorFragosa, Ana
dc.contributor.authorPacheco, Rita
dc.contributor.authorKarmali, Amin
dc.date.accessioned2015-09-08T14:44:06Z
dc.date.available2015-09-08T14:44:06Z
dc.date.issued2012-02
dc.description.abstractThe acetohydroxamic acid synthesis reaction was studied using whole cells, cell-free extract and purified amidase from the strains of Pseudomonas aeruginosa L10 and A13 entrapped in a reverse micelles system composed of cationic surfactant tetradecyltrimethyl ammonium bromide. The specific activity of amidase, yield of synthesis and storage stability were determined for the reversed micellar system as well as for free amidase in conventional buffer medium. The results have revealed that amidase solutions in the reverse micelles system exhibited a substantial increase in specific activity, yield of synthesis and storage stability. In fact, whole cells from P. aeruginosa L10 and AI3 in reverse micellar medium revealed an increase in specific activity of 9.3- and 13.9-fold, respectively, relatively to the buffer medium. Yields of approximately 92% and 66% of acetohydroxamic acid synthesis were obtained for encapsulated cell free extract from P. aeruginosa L10 and A13, respectively. On the other hand, the half-life values obtained for the amidase solutions encapsulated in reverse micelles were overall higher than that obtained for the free amidase solution in buffer medium. Half-life values obtained for encapsulated purified amidase from P. aeruginosa strain L10 and encapsulated cell-free extract from P. aeruginosa strain AI3 were of 17.0 and 26.0 days, respectively. As far as the different sources biocatalyst are concerned, the data presented in this work has revealed that the best results, in both storage stability and biocatalytic efficiency, were obtained when encapsulated cell-free extract from P. aeruginosa strain AI3 at 14/0 of 10 were used. Conformational changes occurring upon encapsulation of both strains enzymes in reverse micelles of TAB in heptane/octanol were additionally identified by FTIR spectroscopy which clarified the biocatalysts performances.por
dc.identifier.citationFRAGOSO, A.; PACHECO, R.; KARMALI, A. – Investigation of structural effects and behaviour of pseudomonas aeruginosa amidase encapsulated in reserved micelles. Process Biochemistry. ISSN: 1359-5113. Vol. 47, nr. 2 (2012), pp. 264-272por
dc.identifier.doi10.1016/j.procbio.2011.11.001
dc.identifier.issn1359-5113
dc.identifier.urihttp://hdl.handle.net/10400.21/5108
dc.language.isoengpor
dc.peerreviewedyespor
dc.publisherElsevier SCI LTDpor
dc.subjectReversed micellespor
dc.subjectPseudomonas aeruginosa amidasespor
dc.subjectAcetohydroxamic Acidpor
dc.subjectWater contentpor
dc.subjectStabilitypor
dc.subjectTransform infrared-spectroscopy
dc.subjectHydroxamic acids
dc.subjectRecombinant amidade
dc.subjectEnzymatic-activity
dc.subjectSystem
dc.subjectFTIR
dc.subjectPurification
dc.subjectPeptides
dc.subjectRoteins
dc.titleInvestigation of structural effects and behaviour of pseudomonas aeruginosa amidase encapsulated in reserved micellespor
dc.typejournal article
dspace.entity.typePublication
oaire.citation.conferencePlaceOxon
oaire.citation.endPage272por
oaire.citation.issue2por
oaire.citation.startPage264por
oaire.citation.titleProcess Biochemistrypor
oaire.citation.volume47por
person.familyNamePacheco
person.familyNameKarmali
person.givenNameRita
person.givenNameAmin
person.identifier1022927
person.identifier.ciencia-id9F13-D310-B5A3
person.identifier.orcid0000-0001-5192-3006
person.identifier.orcid0000-0003-0419-401X
person.identifier.ridC-3062-2012
person.identifier.ridE-4787-2011
person.identifier.scopus-author-id8853708300
person.identifier.scopus-author-id6603778216
rcaap.rightsclosedAccesspor
rcaap.typearticlepor
relation.isAuthorOfPublicationd6907c0a-3f8f-431c-acf2-0b257692f0d4
relation.isAuthorOfPublication23975b4b-3234-4139-9675-89ea6f9a2332
relation.isAuthorOfPublication.latestForDiscoveryd6907c0a-3f8f-431c-acf2-0b257692f0d4

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