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Autor/inn/enGomes, Diana; Sousa, Angela; Passarinha, Lui´s A.
TitelTyrosinase Immobilization in Nickel-Cross-Linked Gellan Microspheres and Conversion of L-DOPA to Dopachrome
QuelleIn: Journal of Chemical Education, 98 (2021) 11, S.3560-3566 (7 Seiten)Infoseite zur Zeitschrift
PDF als Volltext Verfügbarkeit 
Spracheenglisch
Dokumenttypgedruckt; online; Zeitschriftenaufsatz
ISSN0021-9584
DOI10.1021/acs.jchemed.1c00176
SchlagwörterScience Instruction; Science Laboratories; Laboratory Experiments; Science Experiments; Biotechnology; Drug Therapy; Neurological Impairments; Scientific Concepts; Concept Formation; Science Process Skills
AbstractEnzymes are widely applied in different industries, like pharmaceutical, food, biofuel, and waste valorization. However, the enzyme operating conditions are very limited. So, in most industrial processes, enzymes are not efficient, due to the use of harsh conditions, like organic solvents, extreme pH, and temperature. Immobilization arises as a way to overcome the process restrictions by offering better stability, activity, and improved recovery of enzymes. Physical adsorption into a solid support is a simple method to achieve enzyme immobilization and is compatible with different materials, like gellan gum. Tyrosinase is an essential enzyme for the biosynthesis of melanin, flavonoids, and L-DOPA, which is a drug used by the pharmaceutical industry to treat Parkinson's disease. Therefore, it is important to develop an easy and simple method for tyrosinase immobilization that will allow high efficiency and reusability, making the melanin biosynthesis more cost-effective. In the laboratory experiment of the enzymatic biotechnology class, nickel-cross-linked gellan microspheres were prepared and characterized by the students and used as a solid support for tyrosinase immobilization. The reaction catalyzed by tyrosinase was detected by visual observation. This experiment allows students in the biotechnology field to understand the importance of the immobilization process in catalysis since the industry is exploring environmentally friendly processes and also the impact on enzyme efficiency when catalyzing a reaction. Moreover, it helps the students to acquire laboratory handling in the preparation of immobilized systems, while developing their creativity and innovative ability to overcome problems in the enzymatic biotechnology field. (As Provided).
AnmerkungenDivision of Chemical Education, Inc. and ACS Publications Division of the American Chemical Society. 1155 Sixteenth Street NW, Washington, DC 20036. Tel: 800-227-5558; Tel: 202-872-4600; e-mail: eic@jce.acs.org; Web site: http://pubs.acs.org/jchemeduc
Erfasst vonERIC (Education Resources Information Center), Washington, DC
Update2024/1/01
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