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Fucoidan Sulfatases from Marine Bacterium Wenyingzhuangia fucanilytica CZ1127(T)

Fucoidans belong to a structurally heterogeneous class of sulfated polysaccharides isolated from brown algae. They have a wide spectrum of biological activities. The complex structures of these polysaccharides hinder structure-activity relationships determination. Fucoidan sulfatases can make useful...

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Autores principales: Silchenko, Artem S., Rasin, Anton B., Zueva, Anastasiya O., Kusaykin, Mikhail I., Zvyagintseva, Tatiana N., Kalinovsky, Anatoly I., Kurilenko, Valeriya V., Ermakova, Svetlana P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6315715/
https://www.ncbi.nlm.nih.gov/pubmed/30248971
http://dx.doi.org/10.3390/biom8040098
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author Silchenko, Artem S.
Rasin, Anton B.
Zueva, Anastasiya O.
Kusaykin, Mikhail I.
Zvyagintseva, Tatiana N.
Kalinovsky, Anatoly I.
Kurilenko, Valeriya V.
Ermakova, Svetlana P.
author_facet Silchenko, Artem S.
Rasin, Anton B.
Zueva, Anastasiya O.
Kusaykin, Mikhail I.
Zvyagintseva, Tatiana N.
Kalinovsky, Anatoly I.
Kurilenko, Valeriya V.
Ermakova, Svetlana P.
author_sort Silchenko, Artem S.
collection PubMed
description Fucoidans belong to a structurally heterogeneous class of sulfated polysaccharides isolated from brown algae. They have a wide spectrum of biological activities. The complex structures of these polysaccharides hinder structure-activity relationships determination. Fucoidan sulfatases can make useful tools for the determination of the fine chemical structure of fucoidans. In this study, identification and preparation of two recombinant sulfatases able to catalyze the cleavage of sulfate groups from fragments of fucoidan molecules is described for the first time. Two genes of sulfatases swf1 and swf4 of the marine bacterium Wenyingzhuangia fucanilytica CZ1127(T) were cloned and the proteins were produced in Escherichia coli cells. Sulfatases SWF1 and SWF4 are assigned to S1_17 and S1_25 subfamilies of formylglycine-dependent enzymes of S1 family (SulfAtlas). Some molecular and biochemical characteristics of recombinant fucoidan sulfatases have been studied. Detailed specificity and catalytic features of sulfatases were determined using various sulfated fucooligosaccharides. Structures of products produced by SWF1 and SWF4 were established by nuclear magnetic resonance (NMR) spectroscopy. Based on the obtained data, the enzymes are classified as fucoidan exo-2O-sulfatase (SWF1) and fucoidan exo-3O-sulfatase (SWF4). In addition, we demonstrated the sequential action of sulfatases on 2,3-di-O-sulfated fucooligosacchrides, which indicates an exolitic degradation pathway of fucoidan by a marine bacterium W. fucanilytica CZ1127(T).
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spelling pubmed-63157152019-01-10 Fucoidan Sulfatases from Marine Bacterium Wenyingzhuangia fucanilytica CZ1127(T) Silchenko, Artem S. Rasin, Anton B. Zueva, Anastasiya O. Kusaykin, Mikhail I. Zvyagintseva, Tatiana N. Kalinovsky, Anatoly I. Kurilenko, Valeriya V. Ermakova, Svetlana P. Biomolecules Article Fucoidans belong to a structurally heterogeneous class of sulfated polysaccharides isolated from brown algae. They have a wide spectrum of biological activities. The complex structures of these polysaccharides hinder structure-activity relationships determination. Fucoidan sulfatases can make useful tools for the determination of the fine chemical structure of fucoidans. In this study, identification and preparation of two recombinant sulfatases able to catalyze the cleavage of sulfate groups from fragments of fucoidan molecules is described for the first time. Two genes of sulfatases swf1 and swf4 of the marine bacterium Wenyingzhuangia fucanilytica CZ1127(T) were cloned and the proteins were produced in Escherichia coli cells. Sulfatases SWF1 and SWF4 are assigned to S1_17 and S1_25 subfamilies of formylglycine-dependent enzymes of S1 family (SulfAtlas). Some molecular and biochemical characteristics of recombinant fucoidan sulfatases have been studied. Detailed specificity and catalytic features of sulfatases were determined using various sulfated fucooligosaccharides. Structures of products produced by SWF1 and SWF4 were established by nuclear magnetic resonance (NMR) spectroscopy. Based on the obtained data, the enzymes are classified as fucoidan exo-2O-sulfatase (SWF1) and fucoidan exo-3O-sulfatase (SWF4). In addition, we demonstrated the sequential action of sulfatases on 2,3-di-O-sulfated fucooligosacchrides, which indicates an exolitic degradation pathway of fucoidan by a marine bacterium W. fucanilytica CZ1127(T). MDPI 2018-09-21 /pmc/articles/PMC6315715/ /pubmed/30248971 http://dx.doi.org/10.3390/biom8040098 Text en © 2018 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Silchenko, Artem S.
Rasin, Anton B.
Zueva, Anastasiya O.
Kusaykin, Mikhail I.
Zvyagintseva, Tatiana N.
Kalinovsky, Anatoly I.
Kurilenko, Valeriya V.
Ermakova, Svetlana P.
Fucoidan Sulfatases from Marine Bacterium Wenyingzhuangia fucanilytica CZ1127(T)
title Fucoidan Sulfatases from Marine Bacterium Wenyingzhuangia fucanilytica CZ1127(T)
title_full Fucoidan Sulfatases from Marine Bacterium Wenyingzhuangia fucanilytica CZ1127(T)
title_fullStr Fucoidan Sulfatases from Marine Bacterium Wenyingzhuangia fucanilytica CZ1127(T)
title_full_unstemmed Fucoidan Sulfatases from Marine Bacterium Wenyingzhuangia fucanilytica CZ1127(T)
title_short Fucoidan Sulfatases from Marine Bacterium Wenyingzhuangia fucanilytica CZ1127(T)
title_sort fucoidan sulfatases from marine bacterium wenyingzhuangia fucanilytica cz1127(t)
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6315715/
https://www.ncbi.nlm.nih.gov/pubmed/30248971
http://dx.doi.org/10.3390/biom8040098
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