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...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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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. |
format | Online Article Text |
id | pubmed-3736431 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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