Metabolism and enzymology of cyanide/metallocyanide biodegradation by Fusarium solani under neutral and acidic conditions

被引:64
作者
Barclay, M
Tett, VA
Knowles, CJ
机构
[1] Univ Oxford, Dept Engn Sci, Oxford Ctr Environm Biotechnol, Oxford OX1 3PJ, England
[2] Pfizer Ltd, Sandwich CT13 9NJ, Kent, England
基金
英国生物技术与生命科学研究理事会; 英国自然环境研究理事会;
关键词
biodegradation; Fusarium solani; cyanide hydratase; cyanide; metal cyanides; amidase;
D O I
10.1016/S0141-0229(98)00055-6
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
A strain of Fusarium solani degrades metal-complexed cyanides under neutral and acidic pH conditions. Cyanide undergoes hydrolysis to formamide by cyanide hydratase (formamide hydrolyase, EC 4.2.1.66) which is in turn hydrolyzed to ammonia and formic acid by an amidase. The ammonia is their utilized for growth. Formic acid does not accumulate in the medium presumably rifle to its conversion to CO2 by formate dehydrogenase. Cyanide hydratase activity is induced by cyanide or metallocyanides under both acidic and neutral pH conditions, but not by ammonia or formamide; however, the fungus call utilize formamide as the source of nitrogen for growth. F. solani biotransforms K2Ni(CN)(4) and K4Fe(CN)(6) to ammonia under neutral and acidic pH conditions, respectively. The semipurified enzyme has optimal activity for KCN at pH 7.5 and has a K-m of 4.7 mM and a V-max of 1.7 mu mol min(-1) mg(-1) protein. Enzyme purification revealed that the native molecular weight of the enzyme is greater than 300 kDa due to its elution in the void volume during gel filtration, and comprises subunits with a molecular mass of approximately 45 kDa. The N-terminal sequence of the purified cyanide hydratase has a strong homology to previously purified cyanide hydratases, nitrilases, and a cyanidase enzyme. (C) 1998 Elsevier Science Inc.
引用
收藏
页码:321 / 330
页数:10
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