Abstract
As an important glycosaminoglycan hydrolase, chondroitin lyases can hydrolyze chondroitin sulfate (CS) and release disaccharides and oligosaccharides. They are further divided into chondroitin AC, ABC, and B lyases according to their spatial structure and substrate specificity. Chondroitin AC lyase can hydrolyze chondroitin sulfate A (CS-A), chondroitin sulfate C (CS-C), and hyaluronic acid (HA), making it an essential biocatalyst for the preparation of low molecular weight chondroitin sulfate, analysis of the structure of the chondroitin sulfate, treatment of spinal cord injury, and purification of heparin. This paper provides an overview of reported chondroitin AC lyases, including their properties and the challenges faced in industrial applications. Up to now, although many attempts have been adopted to improve the enzyme properties, the most important factors are still the low activity and stability. The relations between the stability of the enzyme and the spatial structure were also summarized and discussed. Also perspectives for remodeling the enzymes with protein engineering are included.









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Abbreviations
- GAGs:
-
Glycosaminoglycans
- CS:
-
Chondroitin sulfate
- HS:
-
Heparin sulfate
- HA:
-
Hyaluronic acid
- DS:
-
Dermatan sulfate
- KS:
-
Keratan sulfate
- GlcA:
-
Glucuronic acid
- GalNAc:
-
N-acetyl-galactosamine
- PL-8:
-
Polysaccharide lyase 8 family
- LMWCS:
-
Low molecular weight chondroitin sulfate
- IdoA:
-
Iduronic acid
- ChSase:
-
Chondroitinase
- GAPDH:
-
Glyceraldehyde 3-phosphate dehydrogenase
- FhchonAC:
-
The chondroitin AC lyase from Flavobacterium heparinum
- CSPGs:
-
Chondroitin sulfate proteoglycans
- DSPGs:
-
Dermatan sulfate-containing proteoglycans
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The financial support from Guangxi Natural Science Foundation (No. 2021GXNSFAA196005) was appreciated.
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The conception and design of this review was from Y-WZ and L-JZ. The first draft of the manuscript was written by X-MF. The manuscript was reviewed by X-MF, J-YH, and Y-WZ.
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Fan, XM., Zhou, LJ., Huang, JY. et al. The structures and applications of microbial chondroitin AC lyase. World J Microbiol Biotechnol 38, 199 (2022). https://doi.org/10.1007/s11274-022-03395-1
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DOI: https://doi.org/10.1007/s11274-022-03395-1

