CER - Central Repository
Institute of Chemistry, Technology and Metallurgy
    • English
    • Српски
    • Српски (Serbia)
  • English 
    • English
    • Serbian (Cyrilic)
    • Serbian (Latin)
  • Login
View Item 
  •   Central Repository
  • IHTM
  • Radovi istraživača / Researchers' publications
  • View Item
  •   Central Repository
  • IHTM
  • Radovi istraživača / Researchers' publications
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

Increased yield of enzymatic synthesis by chromatographic selection of different N-glycoforms of yeast invertase

Thumbnail
2020
Acc_elps.202000092.pdf (1.327Mb)
Authors
Anđelković, Uroš
Gudelj, Ivan
Klarić, Thomas
Hinneburg, Hannes
Vinković, Marijana
Wittine, Karlo
Dovezenski, Nebojša
Vikić-Topić, Dražen
Lauc, Gordan
Vujčić, Zoran
Josić, Đuro
Article (Accepted Version)
,
Wiley-VCH GmbH
Metadata
Show full item record
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 impr...oved 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.

Keywords:
Enzyme stability / Glycoform separation / Monolithic supports / N-glycosylation / Organic solvent
Source:
Electrophoresis, 2020
Publisher:
  • Wiley
Projects:
  • Production, purification and characterization of enzymes and small molecules and their application as soluble or immobilized in food biotechnology, biofuels production and environmental protection (RS-172048)
  • Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200026 (University of Belgrade, Institute of Chemistry, Technology and Metallurgy - IChTM) (RS-200026)
  • HTP-GLYCOMET - Methods for high-throughput glycoproteomic analysis (EU-324400)
  • Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research (EU-256716)
Note:
  • This is the peer-reviewed version of the article: Anđelković, U., Gudelj, I., et. al., Electrophoresis, 2020, https://doi.org/10.1002/elps.202000092
  • The published version: https://cer.ihtm.bg.ac.rs/handle/123456789/3732

DOI: 10.1002/elps.202000092

ISSN: 0173-0835; 1522-2683

PubMed: 33026663

WoS: 000580477100001

Scopus: 2-s2.0-85092915655
[ Google Scholar ]
URI
https://cer.ihtm.bg.ac.rs/handle/123456789/3989
Collections
  • Radovi istraživača / Researchers' publications
Institution
IHTM

DSpace software copyright © 2002-2015  DuraSpace
About CeR – Central Repository | Send Feedback

OpenAIRERCUB
 

 

All of DSpaceInstitutionsAuthorsTitlesSubjectsThis institutionAuthorsTitlesSubjects

Statistics

View Usage Statistics

DSpace software copyright © 2002-2015  DuraSpace
About CeR – Central Repository | Send Feedback

OpenAIRERCUB