Students learned the principles and practice of photometry through project-based learning. They addressed the challenge of measuring the unknown concentration of a colored substance using a photometer they were required to design, build, and test. Then, they used that instrument to carry out the experiment and fulfill the challenge. A photometer was designed and built by students consisting of a green laser pointer as the light source and a lux meter as the detector and readout. Using this photometer students have determined the concentration of the unknown sample of KMnO 4 solutions. The concentration of this sample solution was calculated to be (4.62 ± 0.06) × 10 −4 M; this value agrees within 6% of the expected value from the measurement using the commercial spectrophotometer which was calculated to be (4.96 ± 0.005) × 10 −4 M. The experiments fit well into an analytical chemistry course and take a standard (1 h) lab period. This project has facilitated improved student understanding of the photometry concepts and increased the creative problem-solving. In general, the students' response to this laboratory was positive.
Immobilization of enzymes is one of the most promising methods in enzyme performance enhancement, including stability, recovery, and reusability. However, investigation of suitable solid support in enzyme immobilization is still a scientific challenge. Polyethersulfone (PES) and aminated PES (PES–NH2) were successfully synthesized as novel materials for immobilization. Membranes with various pore sizes (from 10–600 nm) based on synthesized PES and PES–NH2 polymers were successfully fabricated to be applied as bioreactors to increase the immobilized lipase performances. The influence of pore sizes, concentration of additives, and the functional groups that are attached on the PES backbone on enzyme loading and enzyme activity was studied. The largest enzyme loading was obtained by Mucor miehei lipase immobilized onto a PES–NH2 membrane composed of 10% of PES–NH2, 8% of dibutyl phthalate (DBP), and 5% of polyethylene glycol (PEG) (872.62 µg/cm2). Hydrolytic activity of the immobilized lipases indicated that the activities of biocatalysts are not significantly decreased by immobilization. From the reusability test, the lipase immobilized onto PES–NH2 showed a better constancy than the lipase immobilized onto PES (the percent recovery of the activity of the lipases immobilized onto PES–NH2 and PES are 97.16% and 95.37%, respectively), which indicates that this novel material has the potential to be developed as a bioreactor for enzymatic reactions.
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