Literature DB >> 15765216

Removal of aqueous phenol using immobilized enzymes in a bench scale and pilot scale three-phase fluidized bed reactor.

Lucila Ensuncho1, Manuel Alvarez-Cuenca, Raymond L Legge.   

Abstract

The main objective of this work was to investigate the removal of aqueous phenol using immobilized enzymes in both bench scale and pilot scale three-phase fluidized bed reactors. The enzyme used in this application was a fungal tyrosinase [E.C. 1.14.18.1] immobilized in a system of chitosan and alginate. The immobilization matrix consisted of a chitosan matrix cross-linked with glutaraldehyde with an aliginate-filled pore space. This support matrix showed superior mechanical properties along with retaining the unique adsorptive characteristics of the chitosan. Adsorption of the o-quinone product by the chitosan reduced tyrosinase inactivation that is normally observed for this enzyme under these conditions. This approach allowed reuse of the enzyme in repeated batch applications. For the bench scale reactor (1.2-l capacity) more than 92% of the phenol could be removed from the feed water using an immobilized enzyme volume of 18.5% and a residence time of the liquid phase of 150 min. Removal rates decreased with subsequent batch runs. For the pilot scale fluidized bed (60 l), 60% phenol removal was observed with an immobilized enzyme volume of 5% and a residence time of the liquid phase of 7 h. Removal decreased to 45% with a repeat batch run with the same immobilized enzyme.

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Year:  2005        PMID: 15765216     DOI: 10.1007/s00449-005-0400-x

Source DB:  PubMed          Journal:  Bioprocess Biosyst Eng        ISSN: 1615-7591            Impact factor:   3.210


  2 in total

1.  Aspergillus niger PA2 Tyrosinase Covalently Immobilized on a Novel Eco-Friendly Bio-Composite of Chitosan-Gelatin and Its Evaluation for L-DOPA Production.

Authors:  Pragati Agarwal; Swati Dubey; Mukta Singh; Rajesh P Singh
Journal:  Front Microbiol       Date:  2016-12-22       Impact factor: 5.640

2.  High performance microbiological transformation of L-tyrosine to L-dopa by Yarrowia lipolytica NRRL-143.

Authors:  Sikander Ali; Jeffry L Shultz
Journal:  BMC Biotechnol       Date:  2007-08-16       Impact factor: 2.563

  2 in total

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