細菌キシラナーゼに関する研究 (III) : 細菌キシラナーゼの結晶化および若干の酵素化学的性質

概要

論文の詳細を見る
The xylanase of Bac. subtilis G-2 was obtained in a crystalline state and the enzymatic properties were investigated.The results obtained are as follows : 1.The xylanase was fracionally precipitated by a saturation of from 20-60% (NH_4)_2SO_4.2. The enzyme, which had previously been treated with Duolite A-2 to decolor it, was specifically adsorbed into and eluted from Duolite C-10 under certain condition.3. The purified enzyme was easily precipitated with acetone of 60% (v/v). Also, in a dilute acetone solution, the enzyme gradually appeared in a crystalline form. 4. The crystalline enzyme was dissolved in a weak acid solution and recrystallized by adjusting the pH to be slightly alkali.5. The enzyme was stable only between pH 5.0 and 7.0 and at temperatures of less than 45℃.6. The optimum pH for enzyme action was pH 6.0-6.2. The optimum temperature to produce saccharifying and liquefying action on xylan was in the vicinity of 37° and 45℃, respectively, in a thirty minites'test.7. The enzyme activity was increased in the presence of Ca^<++> or Cl^-. However, those ions showed no effect on the stability of the enzyme.8. The enzyme split linkages of xylan by about 38% at the maximum, liberating L-arabinose, xylobiosem xylotriose, and xylosides of other various sizes in the polymerization degree and a very small quantity of free D-xylose.
公益社団法人日本生物工学会の論文
1963-04-15