• 한국식품위생안전성학회지
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• 제11권1호
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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.

• 생명과학회지
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• 제22권12호
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• pp.1724-1728
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• 2012

Ecklonia cava로부터 얻어진 fucoidan을 분해하는 해양세균은 해수로부터 분리하였다. 이 균주의 조효소는 pH8과 $50^{\circ}C$에서 fucoidan을 효율적으로 분해하였다. Crude fucoidanase는 1% (w/v) fucoidan 반응액에서 24시간 내에 약 7.1%를 가수분해하였으며 반응산물로서 endo-type 가수분해에 의한 oligosaccharide를 생산하였다. 16S rRNA 유전자 염기서열분석과 생화학적 시험의 결과로부터 SB 1493균주는 잠정적으로 Pseudoalteromonas sp.로 동정하였다.

• Journal of Microbiology and Biotechnology
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• 제18권4호
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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.