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dc.creatorKnežević-Jugović, Zorica
dc.creatorŽuža, Milena
dc.creatorJakovetić, Sonja
dc.creatorStefanović, Andrea
dc.creatorDžunuzović, Enis
dc.creatorJeremić, Katarina B.
dc.creatorJovanović, Slobodan M.
dc.date.accessioned2021-03-10T13:15:31Z
dc.date.available2021-03-10T13:15:31Z
dc.date.issued2016
dc.identifier.issn8756-7938
dc.identifier.urihttp://TechnoRep.tmf.bg.ac.rs/handle/123456789/3457
dc.description.abstractThe use of penicillin G acylase (PGA) covalently linked to insoluble carrier is expected to produce major advances in pharmaceutical processing industry and the enzyme stability enhancement is still a significant challenge. The objective of this study was to improve catalytic performance of the covalently immobilized PGA on a potential industrial carrier, macroporous poly(glycidyl methacrylate-co-ethylene glycol dimethacrylate) [poly(GMA-co-EGDMA)], by optimizing the copolymerization process and the enzyme attachment procedure. This synthetic copolymer could be a very promising alternative for the development of low-cost, easy-to-prepare, and stable biocatalyst compared to expensive commercially available epoxy carriers such as Eupergit or Sepabeads. The PGA immobilized on poly(GMA-co-EGDMA) in the shape of microbeads obtained by suspension copolymerization appeared to have higher activity yield compared to copolymerization in a cast. Optimal conditions for the immobilization of PGA on poly(GMA-co-EGDMA) microbeads were 1mg/mL of PGA in 0.75mol/L phosphate buffer pH 6.0 at 25 degrees C for 24h, leading to the active biocatalyst with the specific activity of 252.7U/g dry beads. Chemical amination of the immobilized PGA could contribute to the enhanced stability of the biocatalyst by inducing secondary interactions between the enzyme and the carrier, ensuring multipoint attachment. The best balance between the activity yield (51.5%), enzyme loading (25.6mg/g), and stability (stabilization factor 22.2) was achieved for the partially modified PGA.en
dc.publisherWiley, Hoboken
dc.relationinfo:eu-repo/grantAgreement/MESTD/Integrated and Interdisciplinary Research (IIR or III)/46010/RS//
dc.relationEUREKA E!6750
dc.rightsrestrictedAccess
dc.sourceBiotechnology Progress
dc.subjectpenicillin G acylaseen
dc.subjectimmobilizationen
dc.subjectpoly(glycidyl methacrylate-co-ethylene glycol dimethacrylate)en
dc.subjectsuspension copolymerizationen
dc.subjectchemical aminationen
dc.subjectEupergit Cen
dc.titleAn approach for the improved immobilization of penicillin G acylase onto macroporous poly(glycidyl methacrylate-co-ethylene glycol dimethacrylate) as a potential industrial biocatalysten
dc.typearticle
dc.rights.licenseARR
dc.citation.epage53
dc.citation.issue1
dc.citation.other32(1): 43-53
dc.citation.rankM22
dc.citation.spage43
dc.citation.volume32
dc.identifier.doi10.1002/btpr.2181
dc.identifier.pmid26439442
dc.identifier.scopus2-s2.0-84951727521
dc.identifier.wos000371680600006
dc.type.versionpublishedVersion


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Приказ основних података о документу