caa a22 4500 465822231 CHVBK 20180323112138.0 cr unu---uuuuu 170327e19900301xx s 000 0 eng 10.1007/BF00164748 doi (NATIONALLICENCE)springer-10.1007/BF00164748 Decolorization of phenolic effluents by soluble and immobilized phenol oxidases [Elektronische Daten] [Susan Davis, Richard Burns] Summary: Colour removal from phenplic industrial effluents by phenol oxidase enzymes and white-rot fungi was compared. Soluble laccase and horseradish peroxidase (HRP) removed colour from pulp mill (E), cotton mill hydroxide (OH) and cotton mill sulphide (S) effluents, but rapid and irreversible enzyme inactivation took place. Entrapment of laccase in alginate beads improved decolorization by factors of 3.5 (OH) and 2 (E); entrapment of HRP improved decolorization by 36 (OH), 20 (E) and 9 (S). Beads were unsuitable for continuous use because the enzymes were rapidly released into solution. Co-polymerization of laccase or HRP with L-tyrosine gave insoluble polymers with enzyme activity. Entrapment of the co-polymers in gel beads further increased the efficiency of decolorization of E by 28 (laccase) and by 132 (HRP) compared with soluble enzymes. Maximum decolorization of all three effluents by batch cultures of Coriolus versicolor (70%-80% in 8 days) was greater than the maximum enzymic decolorization (48% of OH in 3 days by entrapped laccase). Soluble laccase (222 units ml−1) precipitated 1.2 g l−1 phenol from artificial coal conversion effluent at pH 6.0 and the rate of precipitation and enzyme inactivation was faster at pH 6.0 than at pH 8.5. Springer-Verlag, 1990 Davis Susan Biological Laboratory, University of Kent, CT2 7NJ, Canterbury, Kent, UK aut Burns Richard Biological Laboratory, University of Kent, CT2 7NJ, Canterbury, Kent, UK aut Applied Microbiology and Biotechnology Springer-Verlag 32/6(1990-03-01), 721-726 0175-7598 32:6<721 1990 32 253 https://doi.org/10.1007/BF00164748 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00164748 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Davis Susan Biological Laboratory, University of Kent, CT2 7NJ, Canterbury, Kent, UK aut NATIONALLICENCE 700 1- Burns Richard Biological Laboratory, University of Kent, CT2 7NJ, Canterbury, Kent, UK aut NATIONALLICENCE 773 0- Applied Microbiology and Biotechnology Springer-Verlag 32/6(1990-03-01), 721-726 0175-7598 32:6<721 1990 32 253 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer