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Removal of aqueous phenol and 2‐chlorophenol with purified soybean peroxidase and raw soybean hulls
Author(s) -
Flock Colin,
Bassi Amarjeet,
Gijzen Mark
Publication year - 1999
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/(sici)1097-4660(199904)74:4<303::aid-jctb38>3.0.co;2-b
Subject(s) - phenol , chemistry , hydrogen peroxide , chromatography , batch reactor , peroxidase , aqueous solution , chlorophenol , phenols , raw material , enzyme , organic chemistry , catalysis
In this study, the removal of phenol and 2‐chlorophenolusing soybean seed‐hulls in the presence of hydrogen peroxideis demonstrated. The performance of a stirred membrane reactorcontaining soluble purified SBP was compared with a batch stirredreactor containing raw soybean seed‐hulls. The purified enzymereactor proved to be ineffective while excellent results wereobtained with the crude seed‐hulls for the removal of phenoland 2‐chlorophenol. Four sequential batch reactors containingraw seed‐hulls achieved greater than 96% removal ofphenol with a retention time of 20 min in each reactor. A singlebatch reactor containing raw seed‐hulls was effective inremoving greater than 98.5% of 2‐chlorophenol(initially at 1000 ppm) in less than 15 min. Theperformance of these reactors is comparable to existingHRP‐based technology. The stability of the soybean peroxidase(SBP) enzyme was also examined in the presence ofdetergents (SDS, Tween 20 and Triton X‐100). Lowconcentrations of the detergents significantly increased the enzymeactivity and higher concentrations of detergents (up to20% w/v) did not inactivate the SBP enzyme. Theseresults demonstrate that SBP has good potential for the treatment ofphenol contaminated solutions. © 1999 Society of Chemical Industry