2016
DOI: 10.1093/glycob/cww138
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Expression and biochemical characterization and substrate specificity of the fucoidanase fromFormosa algae

Abstract: A gene that encodes fucoidanase ffa2 in the marine bacterium Formosa algae strain KMM 3553T was cloned, and the protein (FFA2) was produced in Escherichia coli. Recombinant fucoidanase FFA2 was purified, and the biochemical properties of this enzyme were studied. The amino acid sequence of FFA2 showed 57% identity with known fucoidanase FcnA from Mariniflexile fucanivorans. The mass of the gene product FFA2 is 101.2 kDa (918 amino acid residues). Sequence analysis has revealed that fucoidanase FFA2 belongs to … Show more

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Cited by 30 publications
(82 citation statements)
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“…This indicated a hydrolytic activity against a-1,4-linked fucan, since fucans extracted from Laminariales are known to be composed of an a-1,3-linked fucose backbone [2,52]. This is also in agreement with the activities previously observed for the characterized GH107 counterparts, FcnA from M. fucanivorans and FFA2 from F. algae, which were both found to cleave a-1,4-linked fucans [26,27]. Based on the distinct C-PAGE profiles obtained for Fucus serratus, F. vesiculosus, and Fucus spiralis when hydrolyzed with the same fucanase, sulfated fucans seem to be highly structurally diverse, even between closely related algal species.…”
Section: Novel Gh107s Exclusively Degrade Sulfated Fucans Derived Frosupporting
confidence: 90%
See 1 more Smart Citation
“…This indicated a hydrolytic activity against a-1,4-linked fucan, since fucans extracted from Laminariales are known to be composed of an a-1,3-linked fucose backbone [2,52]. This is also in agreement with the activities previously observed for the characterized GH107 counterparts, FcnA from M. fucanivorans and FFA2 from F. algae, which were both found to cleave a-1,4-linked fucans [26,27]. Based on the distinct C-PAGE profiles obtained for Fucus serratus, F. vesiculosus, and Fucus spiralis when hydrolyzed with the same fucanase, sulfated fucans seem to be highly structurally diverse, even between closely related algal species.…”
Section: Novel Gh107s Exclusively Degrade Sulfated Fucans Derived Frosupporting
confidence: 90%
“…These observations give new indications that members of the GH107 family display individual substrate preference for certain algal fucan structures. This may be due to a difference in sulfation, which has previously been found to influence fucanase activity . Yet, additional work is required for confirmation.…”
Section: Resultsmentioning
confidence: 95%
“…Despite the increasing number of publications investigating fucoidanase activity of different marine species cell extracts, few of these enzymes have been isolated and characterized. Moreover, genome sequences encoding few fucoidanases have been published, including Ffa2 and FFA1 from Formosa algae KMM 3553 T [182,183], FcnA from Mariniflexili fucanivorans SW5T [184]. Therefore, specificity of fucoidanases, type of cleaved glycoside bond, structure-activity relationship studies and enzyme stability are still poorly described.…”
Section: Enzymatic Modification Of Native Fucoidansmentioning
confidence: 99%
“…Similarly, recent advances in bioinformatics and genome sequencing of microbial species have resulted in a continual increase of novel genome sequences. These genomes demonstrated various potential genes encoding for enzymes with biopolymer-degrading capabilities, such as Shewanella violacea DSS12 (NC_014012.1), Formosa algae KMM 3553 (NZ_LMAK01000014.1) [182], Formosa haliotis MA1 (NZ_BDEL01000001.1) [198], Wenyingzhuangia fucanilytica CZ1127 (NZ_CP014224.1) [199] and Pseudoalteromonas sp. strain A601 (MXQF01000000) [200].…”
Section: Enzymatic Modification Of Native Fucoidansmentioning
confidence: 99%
“…So, as affected of alkaline fucoidanаse from Littorina kurila yield of LMW sulfated products from F. evanescens which was three times higher compare with action of acid fucoidanase was observed [143,144]. By means of enzymatic hydrolysis of fucoidan from brown alga F. evanescens using of fucoidanase from marine bacteria Formosa algae the product with Mm ~9 kDa was obtained [141,145]. From the results of nuclear magnetic resonance (NMR)-analysis, this fraction represents regular PS, with the following structure of repeating unit:…”
Section: Oligosaccharidesmentioning
confidence: 99%