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KMID : 0525720130180040221
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Journal of Chitin and Chitosan
2013 Volume.18 No. 4 p.221 ~ p.228
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Enzymatic Characterization of α-L-Fucosidase
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Song Ji-Young
Hong Seok-Hwan
Jeong Hyo-Hyeon
Shim Da-Yoon
Lee Min-Jeong
Lee Hyung-Seop
Lee Ji-Hye
Lee Eun-Hye
Park Jae-Kweon
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Abstract
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The aim of the present study is to define the strain that degrade fucoidan as sole carbon source. A bacterium, designated as the strain HH-0518, utilizing fucose was isolated from soil. HH-0518, belonging to the Enterobacteriaceae family by 16S rDNA and physiological analyses, can hydrolyze p-nitropheny-α-L-fucoside (pNP-α-L-fucoside) used as a sole substrate. It was elucidated that α-L-fucosidase of HH-0518 which can hydrolyze pNP-α-L-fucoside was localized on the cell membrane, especially. The α-L-fucosidase appeared to have optimal pH and temperature at 8.0 and 37 o C. Additionally, kinetic parameters of α-L-fucosidase toward artificial substrates pNP-α-L-fucoside were determined to be Km = 1.05 mM and Vmax = 300 pmole/mg/ min, respectively. No significant enzyme activity was observed in the presence of variety of carbon sources including monosaccharides such as galactose, mannose, fructose, sucrose, xylose, glucosamine and N-acetylglucosamine, compared to the medium containing fucoidan only. To the best of our knowledge, we first report the characteristics of α-L-fucosidase from Enterobacter hormaechei strain.
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KEYWORD
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α-L-fucosidase, Fucoidan, N-acetylglucosamine, pNP-α-L-fucoside, 16S rDNA, Enterobacteriaceae
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