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Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase
dc.creator | Anđelković, Uroš | |
dc.creator | Gudelj, Ivan | |
dc.creator | Klarić, Thomas | |
dc.creator | Hinneburg, Hannes | |
dc.creator | Vinković, Marijana | |
dc.creator | Wittine, Karlo | |
dc.creator | Dovezenski, Nebojša | |
dc.creator | Vikić-Topić, Dražen | |
dc.creator | Lauc, Gordan | |
dc.creator | Vujčić, Zoran | |
dc.creator | Josić, Đuro | |
dc.date.accessioned | 2020-12-08T00:28:40Z | |
dc.date.available | 2020-10-08 | |
dc.date.issued | 2020 | |
dc.identifier.issn | 0173-0835 | |
dc.identifier.issn | 1522-2683 | |
dc.identifier.uri | https://cer.ihtm.bg.ac.rs/handle/123456789/3989 | |
dc.description.abstract | Invertases are glycosidases applied for synthesis of alkyl glycosides that are important and effective surfactants. Stability of invertases in the environment with increased content of organic solvent is crucial for increase of productivity of glycosidases. Their stabilityis significantly influenced by N-glycosylation. However, yeast N-glycosylation pathways may synthesize plethora of N-glycan structures. A total natural crude mixture of invertase glycoforms (EINV) extracted from Saccharomyces cerevisiae was subfractionatedby anion-exchange chromatography on industrial monolithic supports to obtain different glycoforms (EINV1–EINV3). Separated glycoforms exhibited different stabilities in wateralcohol solutions that are in direct correlation with the amount of phosphate bound to N-glycans. Observed differences in stability of different invertase glycoforms were used to improve productivity of methyl β-d-fructofuranoside (MF) synthesis. The efficiency and yield of MF synthesis were improved more than 50% when the most stabile glycoform bearing the lowest amount of phosphorylated N-glycans is selected and utilized. These data underline the importance of analysis of glycan structures attached to glycoproteins, demonstrate different impact of N-glycans on the surface charge and enzyme stability inregard to particular reaction environment, and provide a platform for improvement of yield of industrial enzymatic synthesis by chromatographic selection of glycoforms on monolithic supports. | en |
dc.language.iso | en | sr |
dc.publisher | Wiley | sr |
dc.relation | info:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172048/RS// | sr |
dc.relation | info:eu-repo/grantAgreement/MESTD/inst-2020/200026/RS// | sr |
dc.relation | info:eu-repo/grantAgreement/EC/FP7/324400/EU// | sr |
dc.relation | info:eu-repo/grantAgreement/EC/FP7/256716/EU// | sr |
dc.relation.isversionof | https://doi.org/10.1002/elps.202000092 | |
dc.relation.isversionof | https://cer.ihtm.bg.ac.rs/handle/123456789/3732 | |
dc.rights | embargoedAccess | sr |
dc.source | Electrophoresis | sr |
dc.subject | Enzyme stability | sr |
dc.subject | Glycoform separation | sr |
dc.subject | Monolithic supports | sr |
dc.subject | N-glycosylation | sr |
dc.subject | Organic solvent | sr |
dc.title | Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase | en |
dc.type | article | sr |
dc.rights.license | ARR | sr |
dcterms.abstract | Хиннебург, Ханнес; Aнђелковић, Урош; Гудељ, Иван; Кларић, Тхомас; Јосић, Ђуро; Вујчић, Зоран; Лауц, Гордан; Викић-Топић, Дражен; Довезенски, Небојша; Wиттине, Карло; Винковић, Маријана; | |
dc.rights.holder | Wiley-VCH GmbH | sr |
dc.citation.rank | M22~ | |
dc.description.other | This is the peer-reviewed version of the article: Anđelković, U., Gudelj, I., et. al., Electrophoresis, 2020, [https://doi.org/10.1002/elps.202000092] | |
dc.description.other | The published version: [https://cer.ihtm.bg.ac.rs/handle/123456789/3732] | |
dc.identifier.pmid | 33026663 | |
dc.identifier.doi | 10.1002/elps.202000092 | |
dc.identifier.fulltext | https://cer.ihtm.bg.ac.rs/bitstream/id/18384/Acc_elps.202000092.pdf | |
dc.identifier.scopus | 2-s2.0-85092915655 | |
dc.identifier.wos | 000580477100001 | |
dc.type.version | acceptedVersion | sr |