Yanai T, Sato M
Mercian Corporation, Wine & Spirits Research Institute, Fujisawa, Japan.
Biosci Biotechnol Biochem. 2000 Oct;64(10):2179-85. doi: 10.1271/bbb.64.2179.
An intracellular alpha-L-rhamnosidase from Pichia angusta X349 was purified to homogeneity through four chromatographic steps. The alpha-L-rhamnosidase appeared to be a monomeric protein with a molecular mass of 90 kDa. The enzyme had an isoelectric point at 4.9, and was optimally active at pH 6.0 and at around 40 degrees C. The Ki for L-rhamnose inhibition was 25 mM. The enzyme was inhibited by Cu2+, Hg2+, and p-chloromercuribenzoate. The alpha-L-rhamnosidase was highly specific for alpha-L-rhamnopyranoside and liberated rhamnose from naringin, rutin, hesperidin, and 3-quercitrin. The alpha-L-rhamnosidase was active at the ethanol concentrations of wine. It efficiently released monoterpenols, such as linalool and geraniol, from an aroma precursor extracted from Muscat grape juice.
通过四个色谱步骤将来自奥古斯塔毕赤酵母X349的一种细胞内α-L-鼠李糖苷酶纯化至同质。该α-L-鼠李糖苷酶似乎是一种分子量为90 kDa的单体蛋白。该酶的等电点为4.9，在pH 6.0和约40℃时活性最佳。L-鼠李糖抑制的Ki为25 mM。该酶被Cu2+、Hg2+和对氯汞苯甲酸抑制。α-L-鼠李糖苷酶对α-L-鼠李吡喃糖苷具有高度特异性，并从柚皮苷、芦丁、橙皮苷和3-槲皮苷中释放出鼠李糖。该α-L-鼠李糖苷酶在葡萄酒的乙醇浓度下具有活性。它能有效地从麝香葡萄汁中提取的一种香气前体中释放出单萜醇，如芳樟醇和香叶醇。
