Enzyme promiscuity is a concept that in the last years is earning prominence in different fields of enzymology like biocatalysis, enzyme engineering or enzyme evolution. Catalytic promiscuity is defined as the ability of an enzyme to catalyze more than one chemical transformation. Naturally occurring catalytic promiscuity provide the starting point for a Darwinian evolution of enzymes to new fu...

Amphipathic enzymes, invertase (EC 3.2.1.26), 8-amylase (EC 3.2.1.3), and alkaline phosphatase (EC 3.1.3.1), were purified from the rat small intestinal mucosa as trypsin and Triton forms, the catalytic and regulatory characteristics of which were compared in rats and in drosophila. Differences in the catalytic propertiis of the two enzyme forms were demonstrated, which suggested that the hydro...

In this study we report the use of functionalized carbon-based nanomaterials, such as amine-functionalized graphene oxide (GO) and multi-walled carbon nanotubes (CNTs), as effective immobilization supports for various lipases and esterases of industrial interest. Structural and biochemical characterization have revealed that the curvature of the nanomaterial affect the immobilization yield, the...

A hierarchical porous metal-organic framework (MOF), PCN-888, containing three types of cavities was utilized to couple two enzymes into a tandem nanoreactor. The largest cavity (6.2 nm) can only accommodate one molecule of glucose oxidase (GOx). The intermediate cavity (5.0 nm) can accommodate one and only one molecule of horseradish peroxidase (HRP). The small cavity (2.0 nm) has sufficient s...

Growing evidence supports the view that enzymatic activity results from a subtle interplay between chemical kinetics and molecular motions. A systematic analysis is performed here to delineate the type and level of coupling between catalysis and conformational mechanics. The dynamics of a set of 98 enzymes representative of different EC classes are analyzed with the Gaussian network model (GNM)...