Purification and characterization of mandelonitrile lyase from Prunus lyonii.
Purification and characterization of mandelonitrile lyase from Prunus lyonii.
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DOI：
10.1016/0003-9861(86)90733-2
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发表时间：
1986-11
影响因子：
3.9
通讯作者：
Lang-Lai Xu;Bijay K. Singh;Eric E. Conn
中科院分区：
文献类型：
--
作者：
Lang-Lai Xu;Bijay K. Singh;Eric E. Conn
从加利福尼亚樱桃（Prunus lyonii）成熟种子中分离纯化了一种催化苯甲醛氰醇分解的酶——扁桃腈裂解酶（EC 4.1.2.10）。纯化过程包括deae -纤维素和Con-A-Sepharose的层析，最终回收率为60%的酶活性。仅提纯4.3倍就得到了几乎均质的制剂。该蛋白在278、389和463 nm处的吸收光谱最大，表明其为风味蛋白。裂解酶的天然分子量为50,000。在十二烷基硫酸钠存在下，用凝胶电泳法估计其亚基分子量为59,000。等电点估计为4.75。该酶的最佳pH值在5.5左右，在4°C时高度稳定。
The enzyme mandelonitrile lyase (EC 4.1.2.10) which catalyzes the decomposition of the cyanohydrin of benzaldehyde has been isolated and purified to homogeneity from mature seeds of the California cherry (Prunus lyonii). The purification procedure involved chromatography on DEAE-cellulose and Con-A-Sepharose with a final recovery of 60% of enzyme activity. Purification of only 4.3-fold yielded a nearly homogenous preparation. The absorption spectrum of this protein shows maxima at 278, 389, and 463 nm, indicative of its flavoprotein character. The native molecular weight for the lyase was found to be 50,000. The subunit molecular weight of 59,000 was estimated by gel electrophoresis in the presence of sodium dodecylsulfate. The isoelectric point was estimated to be 4.75. The enzyme has a narrow pH optimum around 5.5 and is highly stable at 4 °C.