Thermostable Peroxidase−Polylysine Films for Biocatalysis at 90 °C
Date
2007Author
Guto Peterson M.
Kumar Challa V.
Rusling James F.
Type
ArticleLanguage
enMetadata
Show full item recordAbstract
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/jp071525hhttp://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 9125–9131Publisher
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