Characterization of an Endo-1,3-fucanase from the Glycoside Hydrolase 107 Family.
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| Main Authors: | , , , , , , , |
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| Format: | Artículo científico |
| Language: | en |
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Journal of agricultural and food chemistry
2025
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| _version_ | 1868266174408556544 |
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| author | Yan, Ziyue Liu, Guanchen Chen, Guangning Song, Xiao Zheng, Long Guan, Qing Xue, Changhu Chang, Yaoguang |
| author_facet | Yan, Ziyue Liu, Guanchen Chen, Guangning Song, Xiao Zheng, Long Guan, Qing Xue, Changhu Chang, Yaoguang Yan, Ziyue Liu, Guanchen Chen, Guangning Song, Xiao Zheng, Long Guan, Qing Xue, Changhu Chang, Yaoguang |
| collection | PubMed - marine biology |
| contents | Characterization of an Endo-1,3-fucanase from the Glycoside Hydrolase 107 Family. Yan, Ziyue Liu, Guanchen Chen, Guangning Song, Xiao Zheng, Long Guan, Qing Xue, Changhu Chang, Yaoguang Substrate Specificity Phylogeny Bacterial Proteins Glycoside Hydrolases alpha-L-Fucosidase Hydrogen-Ion Concentration Kinetics Polysaccharides Sulfated fucans are functional polysaccharides derived from marine food, including brown algae and echinoderms, and are widely studied for their nutritional value and bioactive properties. Endo-1,3-fucanases are ideal tools for the research and development of sulfated fucans. However, the current understanding of the subsite specificity of endo-1,3-fucanases from the GH107 family remains limited, which hinders their potential applications of fucanases. This study identified an endo-1,3-fucanase, Fun107Y_Wa, from the GH107 family and performed a detailed analysis, including phylogenetic analysis, molecular biology, enzymology, UPLC-HRMS, and NMR techniques. The catalytic activity of Fun107Y_Wa reached its maximum under conditions of 40 °C and pH 8. Fun107Y_Wa acted in a processive endoacting manner, revealing the catalytic mechanism of endo-1,3-fucanases in GH107. Moreover, Fun107Y_Wa accommodated Fuc(2OSO), Fuc(2OSO), Fuc(2,4OSO), and Fuc at the -2 to +2 subsites. This subsite specificity was distinct from all members of the GH107 family, further clarifying the diversity of subsite specificity of endo-1,3-fucanases from the family. This study enhances the understanding of subsite specificity of endo-1,3-fucanase from the GH107 family, offering a valuable tool for the research and development of sulfated fucans. |
| format | Artículo científico |
| id | pubmed_40705934 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | Journal of agricultural and food chemistry |
| record_format | pubmed |
| spellingShingle | Characterization of an Endo-1,3-fucanase from the Glycoside Hydrolase 107 Family. Yan, Ziyue Liu, Guanchen Chen, Guangning Song, Xiao Zheng, Long Guan, Qing Xue, Changhu Chang, Yaoguang Substrate Specificity Phylogeny Bacterial Proteins Glycoside Hydrolases alpha-L-Fucosidase Hydrogen-Ion Concentration Kinetics Polysaccharides Characterization of an Endo-1,3-fucanase from the Glycoside Hydrolase 107 Family. Yan, Ziyue Liu, Guanchen Chen, Guangning Song, Xiao Zheng, Long Guan, Qing Xue, Changhu Chang, Yaoguang Substrate Specificity Phylogeny Bacterial Proteins Glycoside Hydrolases alpha-L-Fucosidase Hydrogen-Ion Concentration Kinetics Polysaccharides Sulfated fucans are functional polysaccharides derived from marine food, including brown algae and echinoderms, and are widely studied for their nutritional value and bioactive properties. Endo-1,3-fucanases are ideal tools for the research and development of sulfated fucans. However, the current understanding of the subsite specificity of endo-1,3-fucanases from the GH107 family remains limited, which hinders their potential applications of fucanases. This study identified an endo-1,3-fucanase, Fun107Y_Wa, from the GH107 family and performed a detailed analysis, including phylogenetic analysis, molecular biology, enzymology, UPLC-HRMS, and NMR techniques. The catalytic activity of Fun107Y_Wa reached its maximum under conditions of 40 °C and pH 8. Fun107Y_Wa acted in a processive endoacting manner, revealing the catalytic mechanism of endo-1,3-fucanases in GH107. Moreover, Fun107Y_Wa accommodated Fuc(2OSO), Fuc(2OSO), Fuc(2,4OSO), and Fuc at the -2 to +2 subsites. This subsite specificity was distinct from all members of the GH107 family, further clarifying the diversity of subsite specificity of endo-1,3-fucanases from the family. This study enhances the understanding of subsite specificity of endo-1,3-fucanase from the GH107 family, offering a valuable tool for the research and development of sulfated fucans. |
| title | Characterization of an Endo-1,3-fucanase from the Glycoside Hydrolase 107 Family. |
| topic | Substrate Specificity Phylogeny Bacterial Proteins Glycoside Hydrolases alpha-L-Fucosidase Hydrogen-Ion Concentration Kinetics Polysaccharides |
| url | https://pubmed.ncbi.nlm.nih.gov/40705934/ |