N-氨甲酰水解酶的纯化及性质  

Purification and some properties of N-carbamoyl-D-amino acid amidohydrolase

作　　者：李苏平[1] 李家璜[1] 严明[1] 姚忠[1] 朱姝[1] 

机构地区：[1]南京工业大学制药与生命科学学院,南京210009

出　　处：《工业微生物》2005年第1期37-41,共5页Industrial Microbiology

摘　　要：从Burkholderiacepecianjut1分离纯化N氨甲酰D氨基酸水解酶(NDase)。实验表明,该酶亚基35KD,最适温度为52℃,最适pH为7.2左右。以N氨甲酰D苯丙氨酸作底物,其米氏常数Km为10.22mmol/L,最大反应速度Vmax为0.27mmol/(L·min)。实验表明二价金属离子对酶活有重要影响。N-carbamoyl-D-amino acid amidohydrolase from Burkholderia cepecia.njut1was purified . The results showed that the subunit of this enzyme was 35kD.The optimal pH and optimal temperature were 7.2 and 52℃ respectively. The K_m=10.22mmol/L and V_~max =0.27 mmol/(L·min) of the enzyme were obtained by N-carbamoyl-D-phe as the substrate. It also indicated that the bivalent metal ions showed an important influence on the enzyme activity.

关 键 词：酶的纯化 米氏常数 最适PH 最适温度 水解酶 酶活 二价金属离子 KD 实验 左右 

分 类 号：TQ920.1[轻工技术与工程—发酵工程]