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dc.creatorLončar, Nikola
dc.creatorŠokarda Slavić, Marinela
dc.creatorVujčić, Zoran
dc.creatorBožić, Nataša
dc.date.accessioned2019-01-30T17:47:36Z
dc.date.available2019-01-30T17:47:36Z
dc.date.issued2015
dc.identifier.issn2045-2322
dc.identifier.urihttp://cer.ihtm.bg.ac.rs/handle/123456789/1815
dc.description.abstractBacillus licheniformis 9945a alpha-amylase is known as a potent enzyme for raw starch hydrolysis. In this paper, a mixed mode Nuvia cPrime (TM) resin is examined with the aim to improve the downstream processing of raw starch digesting amylases and exploit the hydrophobic patches on their surface. This resin combines hydrophobic interactions with cation exchange groups and as such the presence of salt facilitates hydrophobic interactions while the ion-exchange groups enable proper selectivity. alpha-Amylase was produced using an optimized fed-batch approach in a defined media and significant overexpression of 1.2 g L-1 was achieved. This single step procedure enables simultaneous concentration, pigment removal as well as purification of amylase with yields of 96% directly from the fermentation broth.en
dc.publisherNature Publishing Group, London
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172048/RS//
dc.relationICGEB research project [CRP/YUG11-02]
dc.rightsopenAccess
dc.sourceScientific Reports
dc.titleMixed-mode resins: taking shortcut in downstream processing of raw-starch digesting alpha-amylasesen
dc.typearticle
dc.rights.licenseBY
dcterms.abstractШокарда Славић, Маринела; Божић, Наташа; Вујциц, Зоран; Лонцар, Никола;
dc.citation.volume5
dc.citation.other5:
dc.citation.rankM21
dc.identifier.pmid26492875
dc.identifier.doi10.1038/srep15772
dc.identifier.rcubConv_3430
dc.identifier.fulltexthttp://cer.ihtm.bg.ac.rs//bitstream/id/8256/1813.pdf
dc.identifier.scopus2-s2.0-84945243760
dc.identifier.wos000363430700001
dc.type.versionpublishedVersion


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