Fucoidanase are enzymes that catalyze the conversion of fucoidan into short-chain oligosaccharides through hydrolysis of sugar bonds between fucose or sulfate fucose residues, helping to prepare fucoidan oligosaccharides with high biological activity and clear structure. The use of bioinformatics software to search and identify potential fucoidanase sequences is an important research step to help improve efficiency and save costs in recombinant fucoidanase research. In this paper, we analyze and compare the protein sequence (PF1) originating from the marine bacterium Pseudomonas sp. S3178 with fucoidanase sequences has been published on National Center for Biotechnology Information (NCBI) using bioinformatics software. Analysis results show that PF1 is a protein of 402 amino acids, containing a 22 amino acid signal peptide domain and a 380-amino-acid D1 functional domain typical of fucoidanase. In the D1 domain of PF1, two amino acid residues D203 and H278 have been identified that are responsible for catalysis and four amino acid residues Y142, N144, S231 and T327 belong to the active center of this enzyme. Phylogenetic tree analysis showed that the PF1 sequence belongs to α(1→3) fucoidanase group. These results are the scientific basis and premise for further research to create high-performance, highly active recombinant fucoidanase.
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