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Metabolism of EDTA and its metal chelates by whole cells and cell-free extracts of strain BNC1
Authors:Klüner  T.  Hempel  D. C.  Nörtemann  B.
Affiliation:(1) Institut für Bioverfahrenstechnik, Technische Universit?t Braunschweig, Gauss-Str. 17, D-38106 Braunschweig, Germany Tel.: +49 531 391-7654 Fax: +49 531 391-7652 e-mail: B.Noertemann@tu-bs.de; http://www.tu-bs.de/institute/ibvt, DE
Abstract:The influence of metal ions on the metabolism of ethylenediaminetetraacetate (EDTA) by whole cells and cell-free extracts of strain BNC1 was investigated. Metal-EDTA chelates with thermodynamic stability constants below 1012 were readily mineralized by whole cells with maximum specific turnover rates of 15 (MnEDTA) to 20 (Ca-, Mg-, and BaEDTA) μmol g protein−1 min−1. With the exception of ZnEDTA, chelates with stability constants greater than 1012 were not oxidized at a significant rate. However, it was shown for Fe(III)EDTA that even strong complexes can be degraded after pretreatment by addition of calcium and magnesium salts in the pH range 9–11. The range of EDTA chelates converted by cell-free extracts of strain BNC1 did not depend on their thermodynamic stabilities. The EDTA chelates of Ba2+, Co2+, Mg2+, Mn2+, and Zn2+ were oxidized whereas Ca-, Cd-, Cu-, Fe-, Pb-, and SnEDTA were not. The first catabolic enzyme appears to be an EDTA monooxygenase since it requires O2, NADH, and FMN for its activity and yields glyoxylate and ethylenediaminetriacetate as products. The latter is further degraded via N,N′-ethylenediaminediacetate. The maximum specific turnover rate with MgEDTA, the favoured EDTA species, was 50–130 μmol g protein−1 min−1, and the K m value was 120 μmol/l (K s for whole cells = 8 μmol/l). Whole cells as well as cell-free extracts of strain BNC1 also converted several structural analogues of EDTA. Received: 4 July 1997 / Received revision: 25 September 1997 / Accepted: 29 September 1997
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