PHÂN TÍCH TRÌNH TỰ FUCOIDANASE TIỀM NĂNG CÓ NGUỒN GỐC TỪ CHỦNG VI KHUẨN BIỂN Pseudomonas sp. S3178 BẰNG PHẦN MỀM TIN SINH HỌC

Tóm tắt

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.