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    Thermostable Peroxidase−Polylysine Films for Biocatalysis at 90 °C

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    Date
    2007
    Author
    Guto Peterson M.
    Kumar Challa V.
    Rusling James F.
    Type
    Article
    Language
    en
    Metadata
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    Abstract
    ross-linked films of poly(l-lysine) (PLL) and enzymes covalently linked to surfaces provided remarkable thermostability, enabling biocatalysis at 90 °C. Soret spectra, circular dichroism, and voltammetry showed that PLL films containing peroxidases or myoglobin were stable for up to 9 h at 90 °C, while the same enzymes in solution denatured completely within 20 min. Biocatalytic reduction of t-BuOOH with enzyme-PLL films, using rotating disk voltammetry, provided Michaelis kcat/Km values. Results showed that horseradish peroxidase (HRP)-PLL is 3-fold more active than soybean peroxidase (SBP)-PLL at 25 °C, but SBP-PLL is slightly more active at 90 °C. SBP-PLL films had 8-fold larger kcat/Km values at 90 °C compared to 25 °C. Oxidation of o-methoxyphenol to 3,3‘-dimethoxy-4,4‘-biphenoquinone by peroxidase-PLL-coated silica colloids gave better yields at 90 °C than 25 °C, suggesting increasing catalytic efficiency and selectivity at the higher temperature. These biocolloids were reusable with little loss of activity at 90 °C.
    URI
    http://pubs.acs.org/doi/abs/10.1021/jp071525h
    http://erepository.uonbi.ac.ke:8080/xmlui/handle/123456789/35093
    http://www.ncbi.nlm.nih.gov/pubmed/17608411
    Citation
    J. Phys. Chem. B, 2007, 111 (30), pp 9125–9131
    Publisher
    Department of Pharmacology, University of Connecticut Health Center, Farmington, Connecticu
     
    Department of Chemistry, University of Nairobi, Nairobi
     
    Department of Chemistry and Institute of Materials Science, 55 North Eagleville Road, University of Connecticut, Storrs, Connecticut 06269
     
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    • Faculty of Science & Technology (FST) [4284]

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