Induction and Purification of α-L-Fucosidase from Fusarium oxysporum(Microbiology & Fermentation Industry)

概要

論文の詳細を見る
Fusarium oxysporum highly produced α-L-fucosidase inductively in the culture broth when grown in a medium containing L-fucose, which is the reaction product of the enzyme. Production of the enzyme was also slightly induced by D-arabinose, but not by other sugars including glucose. To efficiently produce the enzyme, the fungus was grown in a glucose medium at first, and then the growing mycelia were transferred to an inducing medium containing only L-fucose. α-L-Fucosidase induced by L-fucose was purified from the inducing medium by fractionation with ammonium sulfate, DEAE-Sephadex A-50 column chromatography and gel filtration on a Sephadex G-100 column. The purified enzyme was judged to be homogeneous on polyacrylamide gel electrophoresis. The enzyme is a glycoprotein with a molecular weight of 75,000. The enzyme can hydrolyze p-nitrophenyl α-L-fucoside, a synthetic substrate, unlike the enzymes of other microorganisms. The Km value for the substrate was 0.48 mM. The optimum pH range was 4.5〜6.0 and the stable pH range 5.5〜10.0. The enzyme hydrolyzed natural substrates such as porcine mucin and fucoidan to produce L-fucose.
社団法人日本農芸化学会の論文
1986-07-23