PURIFICATION OF INACTIVATED PHOTORESPONSIVE NITRILE HYDRATASE

被引:52
作者
NAGAMUNE, T
KURATA, H
HIRATA, M
HONDA, J
KOIKE, H
IKEUCHI, M
INOUE, Y
HIRATA, A
ENDO, I
机构
[1] WASEDA UNIV,SCH SCI & ENGN,SHINJUKU KU,TOKYO 169,JAPAN
[2] RIKEN,SOLAR ENERGY RES GRP,WAKO,SAITAMA 35101,JAPAN
关键词
D O I
10.1016/0006-291X(90)92340-6
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Photoresponsive nitrile hydratase from Rhodococcus sp. N-771 was purified in its inactivated form. The enzyme had a molecular weight of approximately 60 kDa and consisted of 2 subunits each having molecular weight of 27.5 and 28 kDa. The enzyme also contained 2 iron atoms/enzyme as a cofactor. The enzyme was more stable in its inactivated form, rather than the activated during storage in the dark. The enzyme was most stable in the temperature region of 0-35°C, and lost its activity above 40°C. The enzyme was most stable in the pH region of 6-8. The optimum temperature and pH for the enzyme activity was 30°C and 7.8, respectively. The enzyme showed wide substrate specificity, and most of the metal ions did not affect enzyme activity significantly. The absorption spectrum revealed the presence of some cofactor which changed form after photoirradiation. © 1990.
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页码:437 / 442
页数:6
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