酶动力学
酶
米氏-门汀动力学
固定化酶
动力学
化学
基质(水族馆)
位阻效应
营业额
催化作用
反应速率常数
组合化学
酶分析
纳米颗粒
立体化学
有机化学
活动站点
材料科学
纳米技术
生物
生态学
物理
量子力学
出处
期刊:Elsevier eBooks
[Elsevier]
日期:2023-01-01
卷期号:: 133-151
标识
DOI:10.1016/b978-0-323-95074-9.00001-4
摘要
The article focuses on the catalytic activity and stability of enzymes immobilized on nanoparticles (NPs) for antimicrobial dressings and wound healing. The activity of immobilized enzymes is directly related to their performance, which is influenced by the immobilization process on solid supports. This literature review covers the bonding method as well as the different types and materials of NPs. The activity of immobilized enzymes was investigated in the field of enzyme kinetics, which is defined as the rate of enzyme catalysis. We compared the kinetic constants, the Michaelis constant (KM), the maximum reaction rate (Vmax), and the enzyme turnover number (kcat), with native enzymes to see if the enzyme’s affinity to the substrate, and thus the steric availability of the enzyme binding site, did not change after immobilization.
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