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dc.creatorSimović, Milica
dc.creatorVeličković, Dušan
dc.creatorStojanović, Marija
dc.creatorMilosavić, Nenad
dc.creatorRogniaux, Helene
dc.creatorRopartz, David
dc.creatorBezbradica, Dejan
dc.date.accessioned2021-03-10T12:47:00Z
dc.date.available2021-03-10T12:47:00Z
dc.date.issued2015
dc.identifier.issn1359-5113
dc.identifier.urihttp://TechnoRep.tmf.bg.ac.rs/handle/123456789/3018
dc.description.abstractIn this study, enzymatic synthesis of galactoside of salicin, compound with potential physiological activity due to structural resemblance with galectin inhibitors, and analgesic and antipyretic properties of salicin, was performed using beta-galactosidase from Aspergillus oryzae. It was determined, using HPLC and ion mobility mass spectrometry, that enzymatic synthesis was highly selective since only one isomer was formed via primary hydroxyl group on glucose moiety of salicin. The optimization of key experimental factors using response surface methodology enabled galactosyl salicin concentration up to 30.8 mM obtained at lactose concentration 40 mM, salicin concentration 110 mM, enzyme amount 360 IU and reaction time 12 h.en
dc.publisherElsevier Sci Ltd, Oxford
dc.relationinfo:eu-repo/grantAgreement/MESTD/Integrated and Interdisciplinary Research (IIR or III)/46010/RS//
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172049/RS//
dc.rightsrestrictedAccess
dc.sourceProcess Biochemistry
dc.subjectSalicinen
dc.subjectbeta-Galactosidaseen
dc.subjectTransgalactosylationen
dc.subjectresponse surface methodology (RSM)en
dc.subjectIon mobilityen
dc.titleInsight in the regioselective enzymatic transgalactosylation of salicin catalyzed by beta-galactosidase from Aspergillus oryzaeen
dc.typearticle
dc.rights.licenseARR
dc.citation.epage788
dc.citation.issue5
dc.citation.other50(5): 782-788
dc.citation.rankM21
dc.citation.spage782
dc.citation.volume50
dc.identifier.doi10.1016/j.procbio.2015.01.028
dc.identifier.scopus2-s2.0-84939994103
dc.identifier.wos000354147700012
dc.type.versionpublishedVersion


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