Industrial production of glycosaminoglycans
Authors
Datta, Payel
Linhardt, Robert J.
Sharfstein, Susan T.
ORCID
https://orcid.org/0000-0003-2219-5833
No Thumbnail Available
Other Contributors
Issue Date
2019-01-01
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Degree
Terms of Use
In Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/
Full Citation
Industrial production of glycosaminoglycans, P. Datta, R. J. Linhardt, S. T. Sharfstein, Reference Module in Life Sciences 2017, 1-10, 2018.
Abstract
Glycosaminoglycans (GAGs) are naturally occurring polysaccharides, composed of alternating sugar units; these include an amino sugar (e.g., N-acetyl glucosamine, GlcNAc or N-acetyl galactosamine, GalNAc) and either a galactose (Gal) or an uronic acid (GlcA or IdoA) (Fig. 1). The carbon backbone of the GAG chain may undergo no further modifications (e.g., hyaluronan) or may be further modified through sulfation, de-acetylation, and/or epimerization (e.g., heparin, heparan sulfate, chondroitin sulfate, dermatan sulfate and keratan sulfate). Simple non-sulfated GAGs (e.g., hyaluronan) and the precursors of highly sulfated GAGs (e.g., heparosan and chondroitin) are produced in certain bacteria as well as in animals (Cress et al., 2014) These simple GAGs are thought to contribute to pathogenicity of the host bacteria. Simple, non-sulfated GAGs as well as the highly modified sulfated GAGs (e.g., heparin, heparan sulfate, chondroitin sulfate, dermatan sulfate and keratan sulfate) are produced in all animals, including humans. In humans, hyaluronan is part of the connective tissue extracellular matrix (ECM) and is involved in biological functions such as lubrication of joints. Highly sulfated GAGs have tissue-specific sulfated domains that are binding sites for various proteins (Capila and Linhardt, 2002) and, therefore, play critical roles in biological functions such as homeostasis, cell growth, cell migration, development, morphogenesis, tissue repair, and angiogenesis (Linhardt and Toida, 2004; Linhardt, 2003). The current industrial production of GAGs can be broadly classified into three categories: (1) industrial production from animal source, (2) industrial production using microbial cells, and (3) industrial production using eukaryotes. Various GAGs have been routinely extracted and purified from animal sources, for example, hyaluronan from rooster combs, and heparin from pig intestines or bovine lung. An increased knowledge of GAG biosynthesis, as well as the advances in metabolic engineering strategies, bioprocess optimization, downstream processing approaches and analytical tools have led to the production of GAGs from microbial cells and exploration of eukaryotic cells, for example, CHO cells, toward heparin production.
Description
Reference Module in Life Sciences 2017, 1-10
Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Department
The Linhardt Research Labs.
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
Publisher
Relationships
The Linhardt Research Labs Online Collection
Rensselaer Polytechnic Institute, Troy, NY
Encyclopedia of Microbiology
https://harc.rpi.edu/
Rensselaer Polytechnic Institute, Troy, NY
Encyclopedia of Microbiology
https://harc.rpi.edu/
Access
https://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/B978-0-12-809633-8.12224-1