Yokota T, Omori T, Kodama T
J Bacteriol. 1987 Sep;169(9):4049-54. doi: 10.1128/jb.169.9.4049-4054.1987.
A haloalkane dehalogenase was purified to electrophoretic homogeneity from cell extracts of a 1-chlorobutane-utilizing strain, m15-3, which was identified as a Corynebacterium sp. The enzyme hydrolyzed C2 to C12 mono- and dihalogenated alkanes, some haloalcohols, and haloacids. The Km value of the enzyme for 1-chlorobutane was 0.18 mM. Its molecular weight was estimated to be 36,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 33,000 by gel filtration. The isoelectric point was pH 4.5. The optimum pH for enzyme activity was found to be 9.4, and the optimum temperature was 30 to 35 degrees C. The enzyme was stable for 1 h at temperatures ranging from 4 to 30 degrees C but was progressively less stable at 40 and 50 degrees C.
从一株利用1-氯丁烷的菌株m15-3的细胞提取物中纯化出一种卤代烷脱卤酶，该菌株被鉴定为棒状杆菌属。该酶可水解C2至C12的单卤代和二卤代烷烃、一些卤代醇和卤代酸。该酶对1-氯丁烷的Km值为0.18 mM。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳估计其分子量为36,000，通过凝胶过滤估计为33,000。其等电点为pH 4.5。发现酶活性的最佳pH为9.4，最佳温度为30至35摄氏度。该酶在4至30摄氏度的温度下稳定1小时，但在40和50摄氏度时稳定性逐渐降低。
