Int J Biol Macromol 2025 Feb 16;305Pt 2:141171. doi: 10.1016/j.ijbiomac.2025.141171.

A novel endo-1,3-fucanase in glycoside hydrolase family 187 provided a biotechnological tool for preparing sulfated fucan oligosaccharides.

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Sulfated fucan, an important marine polysaccharide frequently presented in echinoderms and brown algae, has gained growing attention owing to its various biological activities. Fucanases are essential tools for degrading sulfated fucan to produce corresponding oligosaccharides. In this context, an endo-1,3-fucanase (Fun187Al) belonging to the GH187 family was successfully expressed in Escherichia coli. Fun187Al showed the highest activity at 30-40 °C and pH 7.5. It hydrolyzed sulfated fucan in a random endo-acting pattern, and displayed a substrate specificity different from the endo-1,3-fucanases of other glycoside hydrolase family. Analyses of ultra-performance liquid chromatography coupled with high-resolution mass spectrometry revealed that tetrasaccharide with two sulfate groups (Fuc4S2), Fuc4S3, and Fuc4S4 were respectively the major components in the end products of Fun187Al against sulfated fucans from Acaudina molpadioides, Thelonota ananas, and Holothuria tubulosa. The capability of Fun187Al to produce oligosaccharides with different degrees of polymerization and sulfation patterns demonstrated that it could be regarded as a favorable tool for establishing the structure-activity relationships of sulfated fucan and its oligosaccharides.

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