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Characterization of a Novel Alginate Lyase with Two Alginate Lyase Domains from the Marine Bacterium Vibrio 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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Autores principales: Sun, Xiao-Meng, Xue, Zhao, Sun, Mei-Ling, Zhang, Yi, Zhang, Yu-Zhong, Fu, Hui-Hui, Zhang, Yu-Qiang, Wang, Peng
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9781882/
https://www.ncbi.nlm.nih.gov/pubmed/36547893
http://dx.doi.org/10.3390/md20120746
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author Sun, Xiao-Meng
Xue, Zhao
Sun, Mei-Ling
Zhang, Yi
Zhang, Yu-Zhong
Fu, Hui-Hui
Zhang, Yu-Qiang
Wang, Peng
author_facet Sun, Xiao-Meng
Xue, Zhao
Sun, Mei-Ling
Zhang, Yi
Zhang, Yu-Zhong
Fu, Hui-Hui
Zhang, Yu-Qiang
Wang, Peng
author_sort Sun, Xiao-Meng
collection PubMed
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 Vibrio 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 Escherichia coli. 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.
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spelling pubmed-97818822022-12-24 Characterization of a Novel Alginate Lyase with Two Alginate Lyase Domains from the Marine Bacterium Vibrio sp. C42 Sun, Xiao-Meng Xue, Zhao Sun, Mei-Ling Zhang, Yi Zhang, Yu-Zhong Fu, Hui-Hui Zhang, Yu-Qiang Wang, Peng Mar Drugs Article 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 Vibrio 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 Escherichia coli. 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. MDPI 2022-11-26 /pmc/articles/PMC9781882/ /pubmed/36547893 http://dx.doi.org/10.3390/md20120746 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Sun, Xiao-Meng
Xue, Zhao
Sun, Mei-Ling
Zhang, Yi
Zhang, Yu-Zhong
Fu, Hui-Hui
Zhang, Yu-Qiang
Wang, Peng
Characterization of a Novel Alginate Lyase with Two Alginate Lyase Domains from the Marine Bacterium Vibrio sp. C42
title Characterization of a Novel Alginate Lyase with Two Alginate Lyase Domains from the Marine Bacterium Vibrio sp. C42
title_full Characterization of a Novel Alginate Lyase with Two Alginate Lyase Domains from the Marine Bacterium Vibrio sp. C42
title_fullStr Characterization of a Novel Alginate Lyase with Two Alginate Lyase Domains from the Marine Bacterium Vibrio sp. C42
title_full_unstemmed Characterization of a Novel Alginate Lyase with Two Alginate Lyase Domains from the Marine Bacterium Vibrio sp. C42
title_short Characterization of a Novel Alginate Lyase with Two Alginate Lyase Domains from the Marine Bacterium Vibrio sp. C42
title_sort characterization of a novel alginate lyase with two alginate lyase domains from the marine bacterium vibrio sp. c42
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9781882/
https://www.ncbi.nlm.nih.gov/pubmed/36547893
http://dx.doi.org/10.3390/md20120746
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