嗜热栖热硫化叶菌39E中耐热环糊精酶的特性分析
Characterization of thermostable cyclodextrinase from Clostridium thermohydrosulfuricum 39E.
作者信息
Saha B C, Zeikus J G
机构信息
Michigan Biotechnology Institute, Lansing 48909.
出版信息
Appl Environ Microbiol. 1990 Sep;56(9):2941-3. doi: 10.1128/aem.56.9.2941-2943.1990.
Abstract
Clostridium thermohydrosulfuricum 39E produced a cell-bound cyclodextrin (CD)-degrading enzyme (cyclodextrinase). It was partially purified 205-fold (specific activity, 14.5 U/mg of protein) by solubilizing with Triton X-100, ammonium sulfate treatment, and DEAE-Sepharose CL-6B column chromatography. The enzyme activity was found to be stable at pH 5.5 and 60 degrees C and optimally active at pH 6.0 and 65 degrees C. The enzyme preparation hydrolyzed CDs, with alpha-CD greater than beta-CD greater than gamma-CD, and displayed a putative multiple attack pattern. The enzyme activity was inhibited by p-chloromercuribenzoate but not by N-bromosuccinimide.
摘要
嗜热硫化氢梭菌39E产生一种细胞结合型环糊精（CD）降解酶（环糊精酶）。通过用Triton X - 100溶解、硫酸铵处理和DEAE - Sepharose CL - 6B柱色谱法，该酶被部分纯化了205倍（比活性为14.5 U/mg蛋白质）。发现该酶活性在pH 5.5和60℃下稳定，在pH 6.0和65℃下活性最佳。该酶制剂能水解环糊精，对α - 环糊精的水解能力大于β - 环糊精大于γ - 环糊精，并呈现出一种假定的多重攻击模式。该酶活性受到对氯汞苯甲酸的抑制，但不受N - 溴代琥珀酰亚胺的抑制。
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