Characterization of a Novel Alginate Lyase with Two Alginate Lyase Domains from the Marine Bacterium <i>Vibrio</i> sp. C42
Alginate is abundant in the cell walls of brown algae. Alginate lyases can degrade alginate, and thus play an important role in the marine carbon cycle and industrial production. Currently, most reported alginate lyases contain only one functional alginate lyase domain. AlyC8 is a putative alginate...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-11-01
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| Series: | Marine Drugs |
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| Online Access: | https://www.mdpi.com/1660-3397/20/12/746 |
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| author | Xiao-Meng Sun Zhao Xue Mei-Ling Sun Yi Zhang Yu-Zhong Zhang Hui-Hui Fu Yu-Qiang Zhang Peng Wang |
| author_facet | Xiao-Meng Sun Zhao Xue Mei-Ling Sun Yi Zhang Yu-Zhong Zhang Hui-Hui Fu Yu-Qiang Zhang Peng Wang |
| author_sort | Xiao-Meng Sun |
| collection | DOAJ |
| description | Alginate is abundant in the cell walls of brown algae. Alginate lyases can degrade alginate, and thus play an important role in the marine carbon cycle and industrial production. Currently, most reported alginate lyases contain only one functional alginate lyase domain. AlyC8 is a putative alginate lyase with two alginate lyase domains (CD1 and CD2) from the marine alginate-degrading strain <i>Vibrio</i> sp. C42. To characterize AlyC8 and its two catalytic domains, AlyC8 and its two catalytic domain-deleted mutants, AlyC8-CD1 and AlyC8-CD2, were expressed in <i>Escherichia coli</i>. All three proteins have noticeable activity toward sodium alginate and exhibit optimal activities at pH 8.0–9.0 and at 30–40 °C, demonstrating that both CD1 and CD2 are functional. However, CD1 and CD2 showed opposite substrate specificity. The differences in substrate specificity and degradation products of alginate between the mutants and AlyC8 demonstrate that CD1 and CD2 can act synergistically to enable AlyC8 to degrade various alginate substrates into smaller oligomeric products. Moreover, kinetic analysis indicated that AlyC8-CD1 plays a major role in the degradation of alginate by AlyC8. These results demonstrate that AlyC8 is a novel alginate lyase with two functional catalytic domains that are synergistic in alginate degradation, which is helpful for a better understanding of alginate lyases and alginate degradation. |
| first_indexed | 2024-03-09T16:09:38Z |
| format | Article |
| id | doaj.art-01fa10fac5254555b1cb20a7d50d696d |
| institution | Directory Open Access Journal |
| issn | 1660-3397 |
| language | English |
| last_indexed | 2024-03-09T16:09:38Z |
| publishDate | 2022-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Marine Drugs |
| spelling | doaj.art-01fa10fac5254555b1cb20a7d50d696d2023-11-24T16:19:29ZengMDPI AGMarine Drugs1660-33972022-11-01201274610.3390/md20120746Characterization of a Novel Alginate Lyase with Two Alginate Lyase Domains from the Marine Bacterium <i>Vibrio</i> sp. C42Xiao-Meng Sun0Zhao Xue1Mei-Ling Sun2Yi Zhang3Yu-Zhong Zhang4Hui-Hui Fu5Yu-Qiang Zhang6Peng Wang7College of Marine Life Sciences, Frontiers Science Center for Deep Ocean Multispheres and Earth System, Ocean University of China, Qingdao 266003, ChinaLife Science College, Shandong Normal University, Jinan 250014, ChinaCollege of Marine Life Sciences, Frontiers Science Center for Deep Ocean Multispheres and Earth System, Ocean University of China, Qingdao 266003, ChinaCollege of Marine Life Sciences, Frontiers Science Center for Deep Ocean Multispheres and Earth System, Ocean University of China, Qingdao 266003, ChinaCollege of Marine Life Sciences, Frontiers Science Center for Deep Ocean Multispheres and Earth System, Ocean University of China, Qingdao 266003, ChinaCollege of Marine Life Sciences, Frontiers Science Center for Deep Ocean Multispheres and Earth System, Ocean University of China, Qingdao 266003, ChinaState Key Laboratory of Microbial Technology, Marine Biotechnology Center, Shandong University, Qingdao 266237, ChinaCollege of Marine Life Sciences, Frontiers Science Center for Deep Ocean Multispheres and Earth System, Ocean University of China, Qingdao 266003, ChinaAlginate is abundant in the cell walls of brown algae. Alginate lyases can degrade alginate, and thus play an important role in the marine carbon cycle and industrial production. Currently, most reported alginate lyases contain only one functional alginate lyase domain. AlyC8 is a putative alginate lyase with two alginate lyase domains (CD1 and CD2) from the marine alginate-degrading strain <i>Vibrio</i> sp. C42. To characterize AlyC8 and its two catalytic domains, AlyC8 and its two catalytic domain-deleted mutants, AlyC8-CD1 and AlyC8-CD2, were expressed in <i>Escherichia coli</i>. All three proteins have noticeable activity toward sodium alginate and exhibit optimal activities at pH 8.0–9.0 and at 30–40 °C, demonstrating that both CD1 and CD2 are functional. However, CD1 and CD2 showed opposite substrate specificity. The differences in substrate specificity and degradation products of alginate between the mutants and AlyC8 demonstrate that CD1 and CD2 can act synergistically to enable AlyC8 to degrade various alginate substrates into smaller oligomeric products. Moreover, kinetic analysis indicated that AlyC8-CD1 plays a major role in the degradation of alginate by AlyC8. These results demonstrate that AlyC8 is a novel alginate lyase with two functional catalytic domains that are synergistic in alginate degradation, which is helpful for a better understanding of alginate lyases and alginate degradation.https://www.mdpi.com/1660-3397/20/12/746alginate lyasecatalytic domainalginate degradationPL7 lyase<i>Vibrio</i>marine bacterium |
| spellingShingle | Xiao-Meng Sun Zhao Xue Mei-Ling Sun Yi Zhang Yu-Zhong Zhang Hui-Hui Fu Yu-Qiang Zhang Peng Wang Characterization of a Novel Alginate Lyase with Two Alginate Lyase Domains from the Marine Bacterium <i>Vibrio</i> sp. C42 Marine Drugs alginate lyase catalytic domain alginate degradation PL7 lyase <i>Vibrio</i> marine bacterium |
| title | Characterization of a Novel Alginate Lyase with Two Alginate Lyase Domains from the Marine Bacterium <i>Vibrio</i> sp. C42 |
| title_full | Characterization of a Novel Alginate Lyase with Two Alginate Lyase Domains from the Marine Bacterium <i>Vibrio</i> sp. C42 |
| title_fullStr | Characterization of a Novel Alginate Lyase with Two Alginate Lyase Domains from the Marine Bacterium <i>Vibrio</i> sp. C42 |
| title_full_unstemmed | Characterization of a Novel Alginate Lyase with Two Alginate Lyase Domains from the Marine Bacterium <i>Vibrio</i> sp. C42 |
| title_short | Characterization of a Novel Alginate Lyase with Two Alginate Lyase Domains from the Marine Bacterium <i>Vibrio</i> sp. C42 |
| title_sort | characterization of a novel alginate lyase with two alginate lyase domains from the marine bacterium i vibrio i sp c42 |
| topic | alginate lyase catalytic domain alginate degradation PL7 lyase <i>Vibrio</i> marine bacterium |
| url | https://www.mdpi.com/1660-3397/20/12/746 |
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