Immobilization of manganese peroxidase from Lentinula edodes and its biocatalytic generation of MnIII-chelate as a chemical oxidant of chlorophenols
✍ Scribed by Anthony C. Grabski; Herbert J. Grimek; Richard R. Burgess
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 185 KB
- Volume
- 60
- Category
- Article
- ISSN
- 0006-3592
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✦ Synopsis
Manganese peroxidase (MnP) purified from commercial cultures of Lentinula edodes was covalently immobilized through its carboxyl groups using an azlactone-functional copolymer derivatized with ethylenediamine and 2-ethoxy-1-ethoxycarbonyl-1,2-dihydroquinoline (EEDQ) as a coupling reagent. The tethered enzyme was employed in a two-stage immobilized MnP bioreactor for catalytic generation of chelated Mn III and subsequent oxidation of chlorophenols. Manganese peroxidase immobilized in the enzyme reactor (reactor 1) produced Mn III -chelate, which was pumped into another chemical reaction vessel (reactor 2) containing the organopollutant. Reactor 1-generated Mn III -chelates oxidized 2,4-dichlorophenol and 2,4,6-trichlorophenol in reactor 2, demonstrating a two-stage enzyme and chemical system. H 2 O 2 and oxalate chelator concentrations were varied to optimize the immobilized MnP's oxidation of Mn II to Mn III . Oxidation of 1.0 mM Mn II to Mn III was initially measured at 78% efficiency under optimized conditions. After 24 h of continuous operation under optimized reaction conditions, the reactor still oxidized 1.0 mM Mn II to Mn III with ∼69% efficiency, corresponding to 88% of the initial MnP activity.