Article ID Journal Published Year Pages File Type
8329119 International Journal of Biological Macromolecules 2017 26 Pages PDF
Abstract
Papain was non-covalently immobilized on multi-walled carbon nanotubes (MWCNTs). Its stabilities and catalytic activity for casein degradation were comprehensively investigated. Compared to free papain, the nano-enzyme exhibited significantly improved thermal, pH and recycling stability. Comparisons of the kinetic parameters between free papain and the heterogeneous enzyme revealed that the Km value of the immobilized papain experienced a slight increase, which suggested that the MWCNTs did not significantly hinder papain's access to substrate or release of product. This feature is beneficial to the industrial applications because of its potential to be easily separated from the end product at the end of the reaction, reuse for multiple times and allow the development of multiple enzyme reaction system.
Related Topics
Life Sciences Biochemistry, Genetics and Molecular Biology Biochemistry
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