Removal of p-alkylphenols from aqueous solutions by combined use of mushroom tyrosinase and chitosan beads

Eazymatic removal of p-alkylphenols from aqueous solutions was investigated through the two-step approach, the quinone conversion of p-alkylphenols with mushroom tyrosinase (EC 1.14.18.1) and the subsequent adsorption of quinone derivatives enzymatically generated on chitosan beads at pH 7.0 and 45...

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Published inBioscience, biotechnology, and biochemistry Vol. 70; no. 10; pp. 2467 - 2475
Main Authors Yamada, K.(Nihon Univ., Narashino, Chiba (Japan). Coll. of Industrial Technology), Inoue, T, Akiba, Y, Kashiwada, A, Matsuda, K, Hirata, M
Format Journal Article
LanguageEnglish
Published Tokyo Japan Society for Bioscience, Biotechnology, and Agrochemistry 01.10.2006
Japan Society for Bioscience Biotechnology and Agrochemistry
Oxford University Press
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Summary:Eazymatic removal of p-alkylphenols from aqueous solutions was investigated through the two-step approach, the quinone conversion of p-alkylphenols with mushroom tyrosinase (EC 1.14.18.1) and the subsequent adsorption of quinone derivatives enzymatically generated on chitosan beads at pH 7.0 and 45 deg C as the optimum conditions. This technique is quite effective for removal of various p-alkylphenols from an aqueous solution. The % removal values of 97-100% were obtained for p-n-alkylphenols with carbon chain lengths of 5 to 9. In addition, removal of other p-alkylphenols was enhanced by increasing either the tyrosinase concentration or the amount of added chitosan beads, and their % removal values reached 93 except for 4-tert-pentylphenol. This technique was also applicable to remove 4-n-octylphenol (4NOP) and 4-n-nonylphenol (4NNP) as suspected endocrine disrupting chemicals. The reaction of quinone derivatives enzymatically generated with the chitosan's amino groups was confirmed by the appearance of peaks for UV-visible spectrum measurements of the chitosan films incubated in the p-alkylphenol and tyrosinase mixture solutions. In addition, 4-tert-pentylphenol underwent tyrosinase-catalyzed oxidation in the presence of hydrogen peroxide.
Bibliography:T01
U30
2007003796
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.60205