1H NMR analysis of perdeutero N-sulfoheparosan C5-epimerization: a direct way to measure the activity of immobilized C5-epimerase. Issue 9 (21st November 2020)

• Record Type: Journal Article
• Authors: Qiao, Meng; Jiao, Ruoyu; Zhang, Xing; Wu, Zhengzhang; Shen, Baoxing; Li, Bingzhi
• Is Part Of: Journal of carbohydrate chemistry. Volume 39:Issue 9(2020)
• Page Start: 437
• Page End: 449
• Publication Date: 2020-11-21
• Subjects: 1H NMR -- C5-epimerase -- immobilized enzyme -- heparan sulfate; Carbohydrates -- Periodicals; 547.78
• DOI: 10.1080/07328303.2021.1903026
• Languages: English
• ISSNs: 0732-8303

Abstract

Abstract: D-Glucuronyl C5-epimerase (C5-epi), which converts D-glucuronic acid to L-iduronic acid, is a crucial enzyme in the preparation of bioengineered heparin, which provides an alternative way to produce safer heparins. Herein, we provided an efficient way to measure the activity of cyanogen bromide-immobilized C5-epi based on proton nuclear magnetic resonance (NMR) analysis of perdeutero N -sulfoheparosan C5-epimerization. In this method, reactions catalyzed by C5-epi could be monitored by real-time 1 D NMR according to the peak intensity change of H-5 from IdoA and GlcA residues in the 1 H NMR spectrum, which is nondestructive of sample and also serves the kinetic property evaluation of immobilized C5-epi. Graphical Abstract: