Hydrolysis of Fucoidan by Fucoidanase Isolated from the Marine Bacterium, Formosa algae

Intracellular fucoidanase was isolated from the marine bacterium, Formosa algae strain KMM 3553. The first appearance of fucoidan enzymatic hydrolysis products in a cell-free extract was detected after 4 h of bacterial growth, and maximal fucoidanase activity was observed after 12 h of growth. The f...

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Autores principales: Silchenko, Artem S., Kusaykin, Mikhail I., Kurilenko, Valeriya V., Zakharenko, Alexander M., Isakov, Vladimir V., Zaporozhets, Tatyana S., Gazha, Anna K., Zvyagintseva, Tatyana N.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2013
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Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3736431/
https://www.ncbi.nlm.nih.gov/pubmed/23852092
http://dx.doi.org/10.3390/md11072413
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author Silchenko, Artem S.
Kusaykin, Mikhail I.
Kurilenko, Valeriya V.
Zakharenko, Alexander M.
Isakov, Vladimir V.
Zaporozhets, Tatyana S.
Gazha, Anna K.
Zvyagintseva, Tatyana N.
author_facet Silchenko, Artem S.
Kusaykin, Mikhail I.
Kurilenko, Valeriya V.
Zakharenko, Alexander M.
Isakov, Vladimir V.
Zaporozhets, Tatyana S.
Gazha, Anna K.
Zvyagintseva, Tatyana N.
author_sort Silchenko, Artem S.
collection PubMed
description Intracellular fucoidanase was isolated from the marine bacterium, Formosa algae strain KMM 3553. The first appearance of fucoidan enzymatic hydrolysis products in a cell-free extract was detected after 4 h of bacterial growth, and maximal fucoidanase activity was observed after 12 h of growth. The fucoidanase displayed maximal activity in a wide range of pH values, from 6.5 to 9.1. The presence of Mg(2+), Ca(2+ )and Ba(2+) cations strongly activated the enzyme; however, Cu(2+) and Zn(2+) cations had inhibitory effects on the enzymatic activity. The enzymatic activity of fucoidanase was considerably reduced after prolonged (about 60 min) incubation of the enzyme solution at 45 °C. The fucoidanase catalyzed the hydrolysis of fucoidans from Fucus evanescens and Fucus vesiculosus, but not from Saccharina cichorioides. The fucoidanase also did not hydrolyze carrageenan. Desulfated fucoidan from F. evanescens was hydrolysed very weakly in contrast to deacetylated fucoidan, which was hydrolysed more actively compared to the native fucoidan from F. evanescens. Analysis of the structure of the enzymatic products showed that the marine bacteria, F. algae, synthesized an α-l-fucanase with an endo-type action that is specific for 1→4-bonds in a polysaccharide molecule built up of alternating three- and four-linked α-l-fucopyranose residues sulfated mainly at position 2.
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spelling pubmed-37364312013-08-07 Hydrolysis of Fucoidan by Fucoidanase Isolated from the Marine Bacterium, Formosa algae Silchenko, Artem S. Kusaykin, Mikhail I. Kurilenko, Valeriya V. Zakharenko, Alexander M. Isakov, Vladimir V. Zaporozhets, Tatyana S. Gazha, Anna K. Zvyagintseva, Tatyana N. Mar Drugs Article Intracellular fucoidanase was isolated from the marine bacterium, Formosa algae strain KMM 3553. The first appearance of fucoidan enzymatic hydrolysis products in a cell-free extract was detected after 4 h of bacterial growth, and maximal fucoidanase activity was observed after 12 h of growth. The fucoidanase displayed maximal activity in a wide range of pH values, from 6.5 to 9.1. The presence of Mg(2+), Ca(2+ )and Ba(2+) cations strongly activated the enzyme; however, Cu(2+) and Zn(2+) cations had inhibitory effects on the enzymatic activity. The enzymatic activity of fucoidanase was considerably reduced after prolonged (about 60 min) incubation of the enzyme solution at 45 °C. The fucoidanase catalyzed the hydrolysis of fucoidans from Fucus evanescens and Fucus vesiculosus, but not from Saccharina cichorioides. The fucoidanase also did not hydrolyze carrageenan. Desulfated fucoidan from F. evanescens was hydrolysed very weakly in contrast to deacetylated fucoidan, which was hydrolysed more actively compared to the native fucoidan from F. evanescens. Analysis of the structure of the enzymatic products showed that the marine bacteria, F. algae, synthesized an α-l-fucanase with an endo-type action that is specific for 1→4-bonds in a polysaccharide molecule built up of alternating three- and four-linked α-l-fucopyranose residues sulfated mainly at position 2. MDPI 2013-07-11 /pmc/articles/PMC3736431/ /pubmed/23852092 http://dx.doi.org/10.3390/md11072413 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0/ This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Silchenko, Artem S.
Kusaykin, Mikhail I.
Kurilenko, Valeriya V.
Zakharenko, Alexander M.
Isakov, Vladimir V.
Zaporozhets, Tatyana S.
Gazha, Anna K.
Zvyagintseva, Tatyana N.
Hydrolysis of Fucoidan by Fucoidanase Isolated from the Marine Bacterium, Formosa algae
title Hydrolysis of Fucoidan by Fucoidanase Isolated from the Marine Bacterium, Formosa algae
title_full Hydrolysis of Fucoidan by Fucoidanase Isolated from the Marine Bacterium, Formosa algae
title_fullStr Hydrolysis of Fucoidan by Fucoidanase Isolated from the Marine Bacterium, Formosa algae
title_full_unstemmed Hydrolysis of Fucoidan by Fucoidanase Isolated from the Marine Bacterium, Formosa algae
title_short Hydrolysis of Fucoidan by Fucoidanase Isolated from the Marine Bacterium, Formosa algae
title_sort hydrolysis of fucoidan by fucoidanase isolated from the marine bacterium, formosa algae
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3736431/
https://www.ncbi.nlm.nih.gov/pubmed/23852092
http://dx.doi.org/10.3390/md11072413
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