Affordable Access

deepdyve-link
Publisher Website

Enzyme immobilization offers a robust tool to scale up the production of longer, diverse, natural glycosaminoglycan oligosaccharides.

Authors
  • Alabbas, Alhumaidi1, 2, 3
  • Desai, Umesh R1, 2
  • 1 Institute for Structural Biology, Drug Discovery and Development, Virginia Commonwealth University, Richmond, VA 23219, USA.
  • 2 Department of Medicinal Chemistry, Virginia Commonwealth University, Richmond, VA 23298, USA.
  • 3 Department of Pharmaceutical Chemistry, Prince Sattam Bin Abdulaziz University, Alkharj 11942, Saudi Arabia. , (Saudi Arabia)
Type
Published Article
Journal
Glycobiology
Publisher
Oxford University Press
Publication Date
Sep 28, 2020
Volume
30
Issue
10
Pages
768–773
Identifiers
DOI: 10.1093/glycob/cwaa027
PMID: 32193533
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Although structurally diverse, longer glycosaminoglycan (GAG) oligosaccharides are critical to understand human biology, few are available. The major bottleneck has been the predominant production of oligosaccharides, primarily disaccharides, upon enzymatic depolymerization of GAGs. In this work, we employ enzyme immobilization to prepare hexasaccharide and longer sequences of chondroitin sulfate in good yields with reasonable homogeneity. Immobilized chondroitinase ABC displayed good efficiency, robust operational pH range, broad thermal stability, high recycle ability and excellent distribution of products in comparison to the free enzyme. Diverse sequences could be chromatographically resolved into well-defined peaks and characterized using LC-MS. Enzyme immobilization technology could enable easier access to diverse longer GAG sequences. © The Author(s) 2020. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: [email protected]

Report this publication

Statistics

Seen <100 times