• Journal of Food Hygiene and Safety
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• v.11 no.1
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• pp.25-29
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• 1996

A fucoidanase, which was screened from the heptopancreas of Patinopectin yessoensis, was fractionated according to by ammounium sulfate precipitation and anion exchange chromatography. The crude fucoidanase activity was hydrolyzed a small amounts of fucoidan agar and not arrageenan. The crude enzyme hydrolyzed fucoidan to produce oligosaccha-rides of fucose, glucose, maltose maltotriose and maltoteraose as the reaction products.

• Journal of Life Science
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• v.22 no.12
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• pp.1724-1728
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• 2012

A marine bacterial strain that degraded fucoidan from Ecklonia cava was isolated from seawater. The crude fucoidanase of this strain efficiently degraded fucoidan at pH 8 and $50^{\circ}C$. The crude enzyme hydrolyzed 7.1% (w/w) fucoidan within 24 hrs from an 1% (w/v) fucoidan solution and produced oligosaccharides by endo-type hydrolysis as the reaction products. The results of 16S rRNA gene sequence analysis and biochemical tests permitted a tentative identification of strain SB 1493 as a Pseudoalteromonas species.

• Journal of Microbiology and Biotechnology
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• v.18 no.4
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• pp.616-623
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• 2008

In spite of an increasing interest in fucoidans as biologically active compounds, no convenient commercial sources with fucoidanase activity are yet available. A marine bacterial strain that showed confluent growth on a minimal medium containing fucoidan, prepared from Korean Undaria pinnatifida sporophylls, as the sole carbon source was isolated and identified based on a 16S rDNA sequence analysis as a strain of Sphingomonas paucimobilis, and named Sphingomonas paucimobilis PF-1. The strain depolymerized fucoidan into more than 7 distinct low-molecular-mass fucose-containing oligosaccharides, ranging from 305 to 3,749 Da. The enzyme activity was shown to be associated with the whole cell, suggesting the possibility of a surface display of the enzyme. However, a whole-cell enzyme preparation neither released the monomer L-fucose from the fucoidan nor hydrolyzed the chromogenic substrate p-nitrophenyl-${\alpha}$-L-fucoside, indicating that the enzyme may be an endo-acting fucoidanase rather than an ${\alpha}$-L-fucosidase. Therefore, this would appear to be the first report on fucoidanolytic activity by a Sphingomonas species and also the first report on the enzymatic degradation of the Korean Undaria pinnatifida sporophyll fucoidan. Moreover, this enzyme activity may be very useful for structural analyses of fucose-containing polysaccharides and the production of bioactive fucooligosaccharides.