Characterization of Bacteroides Species from Human Intestine that Degrades Glycosaminoglycans
Authors
Ahn, M.Y.
Shin, K.H.
Kim, D.H.
Jung, E.A.
Toida, T.
Linhardt, Robert J.
Kim, Y.S.
ORCID
https://orcid.org/0000-0003-2219-5833
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Other Contributors
Issue Date
1998
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Degree
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Full Citation
Characterization of Bacteroides Species from Human Intestinethat Degrades Glycosaminoglycans, M.Y. Ahn, K.H. Shin, D.-H. Kim, E.-A.Jung, T. Toida, R.J. Linhardt, Y.S. Kim, Canadian Journal of Microbiology,44,423-429, 1998.
Abstract
Polysaccharide lyases that can degrade glycosaminoglycans (GAGs) were identified in an anaerobic strain living in the human intestine. The strain was isolated from the stool of a healthy male and identified as Bacteroides sp. strain HJ-15. A detailed taxonomical study indicated the species is a strain of Bacteroides stercoris. The isolate was cultured and the polysaccharide lyase activity was partially purified. This enzyme preparation could act on GAGs containing either glucosamine or galactosamine suggesting the presence of both heparinases and chondroitinases. Various GAGs were incubated with the partially purified enzyme and the products formed were analyzed by strong anion-exchange high performance liquid chromatography and proton nuclear magnetic resonance spectroscopy. These studies demonstrated the presence of at least two types of polysaccharide lyases: heparin lyase and chondroitin sulfate lyase. The eliminative mechanism of these lyase enzymes was confirmed through the isolation of unsaturated disaccharide products. The heparin lyase acted on both heparin and acharan sulfate, a GAG recently isolated from Achatina fulica. The Bacteroides chondroitin lyase, acted on chondroitin sulfates A, B (dermatan sulfate), and C, resembling chondroitin lyase ABC. The presence of a GAG-degrading organism in human intestine may pose problems for the effective oral administration of GAG drugs.
Des polysaccharides lyases capables de d6grader des glycosaminoglycanes (GAGs) ont ete identifiees dans une souche anaerobie vivant dans l'intestin humain. La souche a 6t6 isolee a partir d'excrements d'homme sain et identi iee a Bacteroides sp. HJ-15. Une etude taxonomique d6taill6e a permis d'etablir que ces especes appartenaient A la souche Bacteroides stercoris. Apres isolement, cette souche a ete cultiv6e et l'activite polysaccharide lyase a 6t6 partiellement purifiee. La preparation enzymatique etait active sur des GAGs contenant des glucosamines ou galactosamines, sugg6rant la presence d'h6parinases et de chondroitinases. Differents GAGs ont ete incub6s en presence de l'enzyme partiellement purifiee et les produits formes analyses par chromatographie liquide echangeuse d'anions et par spectroscopie de resonance magnetique nucleaire du proton. Ces etudes ont demontre la presence d'au moins deux types de polysaccharides lyases, soit l'hoparine lyase et la chondroitine sulfate lyase. Le mecanisme d'elimination de ces enzymes lyases a ete confirme par isolement des produits disaccharides insatures. L'heparine lyase etait active sur 1'heparine et l'acharane sulfate, un GAG recemment isole d'Achatina fulica. La chondroitine lyase de Bacteroides fut active sur les chondroitines sulfates A, B (dermatane sulfate) et C. La presence d'un organisme degradant les GAGs dans l'intestin humain est susceptible de poser un probleme pour l'administration orale efficace de medicaments a base de GAGs. Mots cles: Bacteroides stercoris, glycosaminoglycane, spectroscopie de resonance magnetique nucleaire, polysaccharide lyase, heparinase, chondroitinase.
Des polysaccharides lyases capables de d6grader des glycosaminoglycanes (GAGs) ont ete identifiees dans une souche anaerobie vivant dans l'intestin humain. La souche a 6t6 isolee a partir d'excrements d'homme sain et identi iee a Bacteroides sp. HJ-15. Une etude taxonomique d6taill6e a permis d'etablir que ces especes appartenaient A la souche Bacteroides stercoris. Apres isolement, cette souche a ete cultiv6e et l'activite polysaccharide lyase a 6t6 partiellement purifiee. La preparation enzymatique etait active sur des GAGs contenant des glucosamines ou galactosamines, sugg6rant la presence d'h6parinases et de chondroitinases. Differents GAGs ont ete incub6s en presence de l'enzyme partiellement purifiee et les produits formes analyses par chromatographie liquide echangeuse d'anions et par spectroscopie de resonance magnetique nucleaire du proton. Ces etudes ont demontre la presence d'au moins deux types de polysaccharides lyases, soit l'hoparine lyase et la chondroitine sulfate lyase. Le mecanisme d'elimination de ces enzymes lyases a ete confirme par isolement des produits disaccharides insatures. L'heparine lyase etait active sur 1'heparine et l'acharane sulfate, un GAG recemment isole d'Achatina fulica. La chondroitine lyase de Bacteroides fut active sur les chondroitines sulfates A, B (dermatane sulfate) et C. La presence d'un organisme degradant les GAGs dans l'intestin humain est susceptible de poser un probleme pour l'administration orale efficace de medicaments a base de GAGs. Mots cles: Bacteroides stercoris, glycosaminoglycane, spectroscopie de resonance magnetique nucleaire, polysaccharide lyase, heparinase, chondroitinase.
Description
Canadian Journal of Microbiology, 44, 423-429
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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
NRC CNRC
Relationships
The Linhardt Research Labs Online Collection
Rensselaer Polytechnic Institute, Troy, NY
https://harc.rpi.edu/
Rensselaer Polytechnic Institute, Troy, NY
https://harc.rpi.edu/
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