Purification and Properties of Two Galactanases from Penicillium citrinum
スポンサーリンク
概要
- 論文の詳細を見る
Two galactanases (I and II) were purified to homogeneous states from water extracts of a wheat bran culture of Penicillium citrinum. Although these enzymes were separable by affinity chromatography and distinct on polyacrylamide gel electrophoresis, they were similar in physical and enzymatic nature. They had almost the same molecular weight (3.5×104) and isoelectric point (pH 4.2), and similar amino acid compositions and carbohydrate contents (3%). Alanine and leucine were detected for both enzymes as the N- and C-terminal amino acids, respectively. These enzymes were most active at pH 4.5 and 55°C, and were stable between pH 4 and 10 (at 15°C for 24hr), and below 55°C (at pH 5.5 for 10min). The enzymes hydrolyzed soybean arabinogalactan to produce galactose and several galactooligosaccharides, but did not attack coffee bean arabinogalactan. Therefore, these enzymes were suggested to be endo-1, 4-β-D-galactanases. The enzymes also attacked ONPG and PNPG, and lag phases were observed at the beginning of the reactions. Among the compounds examined, Hg2+ and Fe3+ inhibited the enzyme actions. ONPG-hydrolyzing activities of the enzymes were inhibited by some sugars such as lactose, galactose, arabinose, glucose and xylose. Galactobiose, -triose and -tetraose prepared from soybean arabinogalactan with purified galactanase I were found to be further hydrolyzed by the enzymes. A lag phase was also observed in the time course of hydrolysis of galactobiose.
論文 | ランダム
- ケニア--ブラック・アフリカの経済優等生 (世界の中の日本--アフリカ)
- 調査リポート 従業員への事業継承
- 無名人語録(317) (話の特集(第317集))
- 無名人語録 (話の特集(第316集))
- 親子のカタチ(160)永六輔×永麻里