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...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2013-07-01
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| Series: | Marine Drugs |
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| Online Access: | http://www.mdpi.com/1660-3397/11/7/2413 |
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| author | Artem S. Silchenko Mikhail I. Kusaykin Valeriya V. Kurilenko Alexander M. Zakharenko Vladimir V. Isakov Tatyana S. Zaporozhets Anna K. Gazha Tatyana N. Zvyagintseva |
| author_facet | Artem S. Silchenko Mikhail I. Kusaykin Valeriya V. Kurilenko Alexander M. Zakharenko Vladimir V. Isakov Tatyana S. Zaporozhets Anna K. Gazha Tatyana N. Zvyagintseva |
| author_sort | Artem S. Silchenko |
| collection | DOAJ |
| 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 Mg2+, Ca2+ and Ba2+ cations strongly activated the enzyme; however, Cu2+ and Zn2+ 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. |
| first_indexed | 2024-04-14T03:20:07Z |
| format | Article |
| id | doaj.art-73ed305d60f84640a6abae7cd9566a86 |
| institution | Directory Open Access Journal |
| issn | 1660-3397 |
| language | English |
| last_indexed | 2024-04-14T03:20:07Z |
| publishDate | 2013-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Marine Drugs |
| spelling | doaj.art-73ed305d60f84640a6abae7cd9566a862022-12-22T02:15:20ZengMDPI AGMarine Drugs1660-33972013-07-011172413243010.3390/md11072413Hydrolysis of Fucoidan by Fucoidanase Isolated from the Marine Bacterium, Formosa algaeArtem S. SilchenkoMikhail I. KusaykinValeriya V. KurilenkoAlexander M. ZakharenkoVladimir V. IsakovTatyana S. ZaporozhetsAnna K. GazhaTatyana N. ZvyagintsevaIntracellular 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 Mg2+, Ca2+ and Ba2+ cations strongly activated the enzyme; however, Cu2+ and Zn2+ 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.http://www.mdpi.com/1660-3397/11/7/2413fucoidanasefucanasemarine bacteriaFormosa algaefucoidanFucus evanescens |
| spellingShingle | Artem S. Silchenko Mikhail I. Kusaykin Valeriya V. Kurilenko Alexander M. Zakharenko Vladimir V. Isakov Tatyana S. Zaporozhets Anna K. Gazha Tatyana N. Zvyagintseva Hydrolysis of Fucoidan by Fucoidanase Isolated from the Marine Bacterium, Formosa algae Marine Drugs fucoidanase fucanase marine bacteria Formosa algae fucoidan Fucus evanescens |
| 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 | fucoidanase fucanase marine bacteria Formosa algae fucoidan Fucus evanescens |
| url | http://www.mdpi.com/1660-3397/11/7/2413 |
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