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Hydrolysis of α-lactalbumin by cardosin A immobilized on highly activated supports

2003Journal article Open access
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dc.contributor.authorBarros, Rui M.
dc.contributor.authorExtremina, Clara I.
dc.contributor.authorGonçalves, Inês C.
dc.contributor.authorBraga, Beatriz O.
dc.contributor.authorBalcão, Victor M.
dc.contributor.authorMalcata, F. Xavier
dc.date.accessioned2011-10-22T15:46:19Z
dc.date.available2011-10-22T15:46:19Z
dc.date.issued2003
dc.description.abstractIn the present research effort, production of derivatives of cardosin A (a plant protease) encompassing full stabilization of its dimeric structure has been achieved, via covalent, multi-subunit immobilization onto highly activated agarose-glutaraldehyde supports. Boiling such enzyme derivatives in the presence of sodium dodecyl sulfate and β-mercaptoethanol did not lead to leaching of enzyme, thus providing evidence for the effectiveness of the attachment procedure. Furthermore, the cardosin A derivatives prepared under optimal conditions presented ca. half the specific activity of the enzyme in soluble form, and were successfully employed at laboratory-scale trials to perform (selective) hydrolysis of α-lactalbumin (α-La), one of the major proteins in bovine whey. Hydrolysates of α-La were assayed for by the OPA method, as well as by FPLC, SDS–PAGE and HPLC. Thermal inactivation of the immobilized cardosin A was also assessed at 40, 50 and 55 °C; at these temperatures, no thermal denaturation took place during incubation for 48 h. The highest degree of hydrolysis was attained by 5 h reaction, at 55 °C and pH 5.2. SDS–PAGE of α-La hydrolysates displayed bands corresponding to low molecular weight peptides. Our results suggest that cardosin A in immobilized form is a good candidate to bring about proteolysis in the dairy industry, namely in whey processing.por
dc.identifier.citationBARROS, Rui M... [et al.] - Hydrolysis of α-lactalbumin by cardosin A immobilized on highly activated supports. Enzyme and Microbial Technology. ISSN: 0141-0229. Vol. 33, n.º 7 (2003) p. 908-916por
dc.identifier.doi10.1016/S0141-0229(03)00244-8
dc.identifier.urihttp://hdl.handle.net/10400.14/6826
dc.language.isoengpor
dc.peerreviewedyespor
dc.publisherElsevierpor
dc.relation.publisherversionDOI: 10.1016/S0141-0229(03)00244-8por
dc.subjectEnzymepor
dc.subjectProteasepor
dc.subjectAgarosepor
dc.subjectAttachmentpor
dc.subjectStructural stabilizationpor
dc.subjectDairy foodspor
dc.subjectα-Lactalbuminpor
dc.subjectCardosinpor
dc.titleHydrolysis of α-lactalbumin by cardosin A immobilized on highly activated supportspor
dc.typejournal article
dspace.entity.typePublication
person.familyNameBARROS
person.familyNameBalcão
person.familyNameMalcata
person.givenNameRUI
person.givenNameVictor
person.givenNameFrancisco
person.identifier.ciencia-id111D-8A7B-0ED1
person.identifier.ciencia-idC314-A18C-931B
person.identifier.ciencia-id1B13-38A5-35F5
person.identifier.orcid0000-0001-5123-2918
person.identifier.orcid0000-0003-0772-2834
person.identifier.orcid0000-0003-3073-1659
person.identifier.ridJ-3340-2015
person.identifier.ridI-2182-2012
person.identifier.scopus-author-id6603449856
person.identifier.scopus-author-id7102542478
rcaap.rightsopenAccesspor
rcaap.typearticlepor
relation.isAuthorOfPublicationa7bdc538-6d0d-4096-9998-a7be5d07e5d6
relation.isAuthorOfPublication9b0860f7-99b1-4ded-a483-6435882272d0
relation.isAuthorOfPublicationa06c00da-0e2f-4434-8ede-4d7b22c0dfe9
relation.isAuthorOfPublication.latestForDiscoverya06c00da-0e2f-4434-8ede-4d7b22c0dfe9

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