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Soybean hull peroxidase immobilization on macroporous glycidyl methacrylates with different surface characteristics
dc.creator | Prokopijević, Miloš | |
dc.creator | Prodanović, Olivera | |
dc.creator | Spasojević, Dragica | |
dc.creator | Stojanović, Zeljko P | |
dc.creator | Radotić, Ksenija | |
dc.creator | Prodanović, Radivoje | |
dc.date.accessioned | 2022-04-05T14:48:35Z | |
dc.date.available | 2022-04-05T14:48:35Z | |
dc.date.issued | 2014 | |
dc.identifier.issn | 1615-7591 | |
dc.identifier.uri | http://rimsi.imsi.bg.ac.rs/handle/123456789/754 | |
dc.description.abstract | Soybean hull peroxidase (SHP, E.C. 1.11.1.7) was immobilized by a glutaraldehyde and periodate method onto series of macroporous copolymers of glycidyl methacrylate (GMA) and ethylene glycol dimethacrylate (EGDMA), poly(GMA-co-EGDMA) with various surface characteristics and pore size diameters ranging from 44 to 200 nm. Glutaraldehyde immobilization method and poly(GMA-co-EGDMA) named SGE 20/12 with pore sizes of 120 nm gave immobilized enzyme with highest specific activity of 25 U/g. Deactivation studies showed that immobilization increased stability of SHP and that surface characteristics of the used copolymer had a major influence on a stability of immobilized enzyme at high temperatures and in an organic solvent. The highest thermostability was obtained using the copolymer SGE 20/12 with pore size of 120 nm, while the highest stability in dioxane had SHP immobilized onto copolymer SGE 10/4 with pore size of 44 nm. Immobilized SHP showed a wider pH optimum as compared to the native enzyme especially at alkaline pH values and 3.2 times increased K (m) value for pyrogallol. After 6 cycles of repeated use in batch reactor, immobilized SHP retained 25 % of its original activity. Macroporous copolymers with different surface characteristics can be used for fine tuning of activity and stability of immobilized SHP to obtain a biocatalyst suitable for phenol oxidation or polymer synthesis in organic solvents. | en |
dc.publisher | Springer, New York | |
dc.relation | info:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/173017/RS// | |
dc.relation | info:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172049/RS// | |
dc.rights | restrictedAccess | |
dc.source | Bioprocess and Biosystems Engineering | |
dc.subject | Stability | en |
dc.subject | Periodate | en |
dc.subject | Immobilized enzyme | en |
dc.subject | Glutaraldehyde | en |
dc.subject | Copolymer | en |
dc.title | Soybean hull peroxidase immobilization on macroporous glycidyl methacrylates with different surface characteristics | en |
dc.type | article | |
dc.rights.license | ARR | |
dc.citation.epage | 804 | |
dc.citation.issue | 5 | |
dc.citation.other | 37(5): 799-804 | |
dc.citation.rank | M22 | |
dc.citation.spage | 799 | |
dc.citation.volume | 37 | |
dc.identifier.doi | 10.1007/s00449-013-1050-z | |
dc.identifier.pmid | 24061564 | |
dc.identifier.scopus | 2-s2.0-84905649784 | |
dc.identifier.wos | 000334932300005 | |
dc.type.version | publishedVersion |