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.
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