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Expression, Purification and Characterization of Chondroitinase AC II from Marine Bacterium Arthrobacter sp. CS01
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| Zeitschriftentitel: | Marine Drugs |
|---|---|
| Personen und Körperschaften: | , , , , , , , |
| In: | Marine Drugs, 17, 2019, 3, S. 185 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
MDPI AG
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| Schlagwörter: |
| author_facet |
Fang, Yangtao Yang, Suxiao Fu, Xiaodan Xie, Wancui Li, Li Liu, Zhemin Mou, Haijin Zhu, Changliang Fang, Yangtao Yang, Suxiao Fu, Xiaodan Xie, Wancui Li, Li Liu, Zhemin Mou, Haijin Zhu, Changliang |
|---|---|
| author |
Fang, Yangtao Yang, Suxiao Fu, Xiaodan Xie, Wancui Li, Li Liu, Zhemin Mou, Haijin Zhu, Changliang |
| spellingShingle |
Fang, Yangtao Yang, Suxiao Fu, Xiaodan Xie, Wancui Li, Li Liu, Zhemin Mou, Haijin Zhu, Changliang Marine Drugs Expression, Purification and Characterization of Chondroitinase AC II from Marine Bacterium Arthrobacter sp. CS01 Drug Discovery Pharmacology, Toxicology and Pharmaceutics (miscellaneous) Pharmaceutical Science |
| author_sort |
fang, yangtao |
| spelling |
Fang, Yangtao Yang, Suxiao Fu, Xiaodan Xie, Wancui Li, Li Liu, Zhemin Mou, Haijin Zhu, Changliang 1660-3397 MDPI AG Drug Discovery Pharmacology, Toxicology and Pharmaceutics (miscellaneous) Pharmaceutical Science http://dx.doi.org/10.3390/md17030185 <jats:p>Chondroitinase (ChSase), a type of glycosaminoglycan (GAG) lyase, can degrade chondroitin sulfate (CS) to unsaturate oligosaccharides, with various functional activities. In this study, ChSase AC II from a newly isolated marine bacterium Arthrobacter sp. CS01 was cloned, expressed in Pichia pastoris X33, purified, and characterized. ChSase AC II, with a molecular weight of approximately 100 kDa and a specific activity of 18.7 U/mg, showed the highest activity at 37 °C and pH 6.5 and maintained stability at a broad range of pH (5–7.5) and temperature (below 35 °C). The enzyme activity was increased in the presence of Mn2+ and was strongly inhibited by Hg2+. Moreover, the kinetic parameters of ChSase AC II against CS-A, CS-C, and HA were determined. TLC and ESI-MS analysis of the degradation products indicated that ChSase AC II displayed an exolytic action mode and completely hydrolyzed three substrates into oligosaccharides with low degrees of polymerization (DPs). All these features make ChSase AC II a promising candidate for the full use of GAG to produce oligosaccharides.</jats:p> Expression, Purification and Characterization of Chondroitinase AC II from Marine Bacterium Arthrobacter sp. CS01 Marine Drugs |
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| title |
Expression, Purification and Characterization of Chondroitinase AC II from Marine Bacterium Arthrobacter sp. CS01 |
| title_unstemmed |
Expression, Purification and Characterization of Chondroitinase AC II from Marine Bacterium Arthrobacter sp. CS01 |
| title_full |
Expression, Purification and Characterization of Chondroitinase AC II from Marine Bacterium Arthrobacter sp. CS01 |
| title_fullStr |
Expression, Purification and Characterization of Chondroitinase AC II from Marine Bacterium Arthrobacter sp. CS01 |
| title_full_unstemmed |
Expression, Purification and Characterization of Chondroitinase AC II from Marine Bacterium Arthrobacter sp. CS01 |
| title_short |
Expression, Purification and Characterization of Chondroitinase AC II from Marine Bacterium Arthrobacter sp. CS01 |
| title_sort |
expression, purification and characterization of chondroitinase ac ii from marine bacterium arthrobacter sp. cs01 |
| topic |
Drug Discovery Pharmacology, Toxicology and Pharmaceutics (miscellaneous) Pharmaceutical Science |
| url |
http://dx.doi.org/10.3390/md17030185 |
| publishDate |
2019 |
| physical |
185 |
| description |
<jats:p>Chondroitinase (ChSase), a type of glycosaminoglycan (GAG) lyase, can degrade chondroitin sulfate (CS) to unsaturate oligosaccharides, with various functional activities. In this study, ChSase AC II from a newly isolated marine bacterium Arthrobacter sp. CS01 was cloned, expressed in Pichia pastoris X33, purified, and characterized. ChSase AC II, with a molecular weight of approximately 100 kDa and a specific activity of 18.7 U/mg, showed the highest activity at 37 °C and pH 6.5 and maintained stability at a broad range of pH (5–7.5) and temperature (below 35 °C). The enzyme activity was increased in the presence of Mn2+ and was strongly inhibited by Hg2+. Moreover, the kinetic parameters of ChSase AC II against CS-A, CS-C, and HA were determined. TLC and ESI-MS analysis of the degradation products indicated that ChSase AC II displayed an exolytic action mode and completely hydrolyzed three substrates into oligosaccharides with low degrees of polymerization (DPs). All these features make ChSase AC II a promising candidate for the full use of GAG to produce oligosaccharides.</jats:p> |
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| author | Fang, Yangtao, Yang, Suxiao, Fu, Xiaodan, Xie, Wancui, Li, Li, Liu, Zhemin, Mou, Haijin, Zhu, Changliang |
| author_facet | Fang, Yangtao, Yang, Suxiao, Fu, Xiaodan, Xie, Wancui, Li, Li, Liu, Zhemin, Mou, Haijin, Zhu, Changliang, Fang, Yangtao, Yang, Suxiao, Fu, Xiaodan, Xie, Wancui, Li, Li, Liu, Zhemin, Mou, Haijin, Zhu, Changliang |
| author_sort | fang, yangtao |
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| description | <jats:p>Chondroitinase (ChSase), a type of glycosaminoglycan (GAG) lyase, can degrade chondroitin sulfate (CS) to unsaturate oligosaccharides, with various functional activities. In this study, ChSase AC II from a newly isolated marine bacterium Arthrobacter sp. CS01 was cloned, expressed in Pichia pastoris X33, purified, and characterized. ChSase AC II, with a molecular weight of approximately 100 kDa and a specific activity of 18.7 U/mg, showed the highest activity at 37 °C and pH 6.5 and maintained stability at a broad range of pH (5–7.5) and temperature (below 35 °C). The enzyme activity was increased in the presence of Mn2+ and was strongly inhibited by Hg2+. Moreover, the kinetic parameters of ChSase AC II against CS-A, CS-C, and HA were determined. TLC and ESI-MS analysis of the degradation products indicated that ChSase AC II displayed an exolytic action mode and completely hydrolyzed three substrates into oligosaccharides with low degrees of polymerization (DPs). All these features make ChSase AC II a promising candidate for the full use of GAG to produce oligosaccharides.</jats:p> |
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| spelling | Fang, Yangtao Yang, Suxiao Fu, Xiaodan Xie, Wancui Li, Li Liu, Zhemin Mou, Haijin Zhu, Changliang 1660-3397 MDPI AG Drug Discovery Pharmacology, Toxicology and Pharmaceutics (miscellaneous) Pharmaceutical Science http://dx.doi.org/10.3390/md17030185 <jats:p>Chondroitinase (ChSase), a type of glycosaminoglycan (GAG) lyase, can degrade chondroitin sulfate (CS) to unsaturate oligosaccharides, with various functional activities. In this study, ChSase AC II from a newly isolated marine bacterium Arthrobacter sp. CS01 was cloned, expressed in Pichia pastoris X33, purified, and characterized. ChSase AC II, with a molecular weight of approximately 100 kDa and a specific activity of 18.7 U/mg, showed the highest activity at 37 °C and pH 6.5 and maintained stability at a broad range of pH (5–7.5) and temperature (below 35 °C). The enzyme activity was increased in the presence of Mn2+ and was strongly inhibited by Hg2+. Moreover, the kinetic parameters of ChSase AC II against CS-A, CS-C, and HA were determined. TLC and ESI-MS analysis of the degradation products indicated that ChSase AC II displayed an exolytic action mode and completely hydrolyzed three substrates into oligosaccharides with low degrees of polymerization (DPs). All these features make ChSase AC II a promising candidate for the full use of GAG to produce oligosaccharides.</jats:p> Expression, Purification and Characterization of Chondroitinase AC II from Marine Bacterium Arthrobacter sp. CS01 Marine Drugs |
| spellingShingle | Fang, Yangtao, Yang, Suxiao, Fu, Xiaodan, Xie, Wancui, Li, Li, Liu, Zhemin, Mou, Haijin, Zhu, Changliang, Marine Drugs, Expression, Purification and Characterization of Chondroitinase AC II from Marine Bacterium Arthrobacter sp. CS01, Drug Discovery, Pharmacology, Toxicology and Pharmaceutics (miscellaneous), Pharmaceutical Science |
| title | Expression, Purification and Characterization of Chondroitinase AC II from Marine Bacterium Arthrobacter sp. CS01 |
| title_full | Expression, Purification and Characterization of Chondroitinase AC II from Marine Bacterium Arthrobacter sp. CS01 |
| title_fullStr | Expression, Purification and Characterization of Chondroitinase AC II from Marine Bacterium Arthrobacter sp. CS01 |
| title_full_unstemmed | Expression, Purification and Characterization of Chondroitinase AC II from Marine Bacterium Arthrobacter sp. CS01 |
| title_short | Expression, Purification and Characterization of Chondroitinase AC II from Marine Bacterium Arthrobacter sp. CS01 |
| title_sort | expression, purification and characterization of chondroitinase ac ii from marine bacterium arthrobacter sp. cs01 |
| title_unstemmed | Expression, Purification and Characterization of Chondroitinase AC II from Marine Bacterium Arthrobacter sp. CS01 |
| topic | Drug Discovery, Pharmacology, Toxicology and Pharmaceutics (miscellaneous), Pharmaceutical Science |
| url | http://dx.doi.org/10.3390/md17030185 |