Journal
JOURNAL OF THE IRANIAN CHEMICAL SOCIETY
Volume 19, Issue 6, Pages 2115-2130Publisher
SPRINGER
DOI: 10.1007/s13738-021-02449-9
Keywords
Enzyme immobilization; Enzyme stability; Ugi multicomponent reaction; Material chemistry; Green chemistry
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Enzymes play a key role in chemical industries as biological catalysts. Immobilization of enzymes using techniques like the Ugi multicomponent reaction can enhance their stability and activity, leading to a more robust catalyst system. Immobilized enzymes through Ugi MCR show good stability and activity, with the potential for synergistic effects on enzyme activities.
Enzymes play a key role in the most prominent chemical industries as biological catalysts. Based on current demands of the chemical industries in enzyme productivity and development, many techniques were utilized to increase their shelf life and activities by immobilization of enzymes. The heterogeneous (immobilized) enzymes provide a reusable catalyst system that is more robust and more stable than free enzymes under various environmental conditions. In this review, we attempt to underscore the applications of Ugi multicomponent reaction (MCR) in the immobilization of enzymes on various organic and inorganic supports such as polymers, carbon allotropes, and inorganic materials. Our study showed that enzymes immobilized via Ugi MCRs show good stabilities and activities. In addition, the biological potentials of the dipeptide structures immobilized by Ugi MCR can emerge as a synergistic effect on the enzyme activities.
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