Biocatalysis with Sol−Gel Encapsulated Acid Phosphatase
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Suhasini Kulkarni [1] ; Vu Tran [1] ; Maggie K. M. Ho [1] ; Chieu Phan [1] ; Elizabeth Chin [1] ; Zeke Wemmer [1] ; Monika Sommerhalter [1]
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[1] California State University
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- Localización: Journal of chemical education, ISSN 0021-9584, Vol. 87, Nº 9 (September), 2010, págs. 958-960
- Idioma: inglés
- Texto completo no disponible (Saber más ...)
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Resumen
This experiment was performed in an upper-level undergraduate biochemistry laboratory course. Students learned how to immobilize an enzyme in a sol−gel matrix and how to perform and evaluate enzyme-activity measurements. The enzyme acid phosphatase (APase) from wheat germ was encapsulated in sol−gel beads that were prepared from the precursor molecule tetramethoxysilane. The enzymatic activities of free and immobilized APase were measured with a colorimetric assay that monitors the formation of p-nitrophenolate from p-nitrophenylphosphate. Students critically assessed the advantages and disadvantages of sol−gel based enzyme immobilization by investigating the catalytic performance, the enzyme retention, and the reuse capability of the APase sol−gel beads. This experiment exposed students to thoughts and techniques that are important for the biotechnological application of enzymes.
