Mild hydrolysis of nitriles by the immobilized nitrilase from Aspergillus niger K10

被引:28
作者
Vejvoda, V
Kaplan, O
Bezouska, K
Martínková, L
机构
[1] Acad Sci Czech Republ, Inst Microbiol, Lab Biotransformat, CZ-14220 Prague, Czech Republic
[2] Charles Univ, Fac Sci, Dept Biochem, CZ-12840 Prague, Czech Republic
关键词
nitrilase; Aspergillus niger; benzonitrile; cyanopyridines; immobilized enzyme;
D O I
10.1016/j.molcatb.2006.01.027
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
The cell free extract front the nitrile-hydrolyzing strain Aspergillus niger K10 (0.25 mg of protein) was adsorped onto a 1 mL HiTrap Butyl Sepharose column. The benzonitrile-hydrolyzing activity of the immobilized enzyme (about 1.6 U/mg of protein) was stable at pH 8 and 35 degrees C within the examined period (4 h). The enzyme load on the above column was increased 18 times in order to achieve high nitrile conversion. This enzyme preparation was used for the conversion of 3-cyanopyridine and 4-cyanopyridine under the above conditions. The initial substrate conversion was nearly quantitative. The activity was fairly stable; the conversion of 3-cyanopyridine decreased to 70% after 15 h, while the conversion of 4-cyanopyridine was 60% of the initial value after 39 It. The former substrate was converted into nicotinic acid and nicotinamide (molar ratio approximately 16: 1) and the latter one into isonicotinic acid and isonicotinamide (molar ratio approximately 3: 1 (c) 2006 Elsevier B.V. All rights reserved.
引用
收藏
页码:55 / 58
页数:4
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