Improved recovery of active recombinant laccase from maize seed
| Autor: | Michele Bailey, Maria E Magallanes-Lundback, John Howard, E. Callaway, D. D. Delaney, Michael E. Horn, Elizabeth E. Hood, Susan L. Woodard, Jeff Lane, Mick Ward, H. Mallubhotla, F. Van Gastel, Katherine K. Beifuss |
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| Rok vydání: | 2003 |
| Předmět: |
chemistry.chemical_element
Applied Microbiology and Biotechnology Chloride Lignin Zea mays Fungal Proteins chemistry.chemical_compound Apoenzymes Dry weight Chlorides medicine Laccase chemistry.chemical_classification Fungal protein Chromatography General Medicine Plants Genetically Modified Copper Recombinant Proteins Enzyme chemistry Polymerization Biochemistry Seeds Polyporales Biotechnology medicine.drug |
| Zdroj: | Applied microbiology and biotechnology. 63(4) |
| ISSN: | 0175-7598 |
| Popis: | Lignolytic enzymes such as laccase have been difficult to over-express in an active form. This paper describes the expression, characterization, and application of a fungal laccase in maize seed. The transgenic seed contains immobilized and extractable laccase. Fifty ppm dry weight of aqueously extractable laccase was obtained, and the remaining solids contained a significant amount of immobilized laccase that was active. Although a portion of the extractable laccase was produced as inactive apoenzyme, laccase activity was recovered by treatment with copper and chloride. In addition to allowing the apoenzyme to regain activity, treatment with copper also provided a partial purification step by precipitating other endogenous corn proteins while leaving >90% of the laccase in solution. The data also demonstrate the application of maize-produced laccase as a polymerization agent. The apparent concentration of laccase in ground, defatted corn germ is approximately 0.20% of dry weight. |
| Databáze: | OpenAIRE |
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