Kinetic Modelling of Enzyme Catalyzed Biotransformation Involving Activations and Inhibitions

Abstract

To achieve transition from lab scale enzyme studies to industrial applications, understanding of enzyme kinetics plays a critical role. The widely applied Michaelis Menten equation of the single substrate kinetics, sequential and double replacement mechanism of bisubstrate reaction and the relevant kinetics, inhibition and activation of enzyme are all integral parts of this discussion. In this chapter, we have discussed different types of inhibition and kinetic modelling. Systematic approach to generate data and its interpretation as well as designing of inhibitors is also explained.

Protein inorganic hybrid nanoflowers of a microbial carbonic anhydrase as efficient tool for the conversion of CO2 into value added product

“…In the previous study, the V max value of β‐glucosidase immobilized in alginate beads decreased from 0.94 μmol min −1 mL −1 to 0.74 μmol min −1 mL −1 48 . The decrease in V max after immobilization is most likely due to the interaction of the biocatalyst with functional moieties present on the surface of the matrices 53 …”

“…48 The decrease in V max after immobilization is most likely due to the interaction of the biocatalyst with functional moieties present on the surface of the matrices. 53 Stability and reusability of CANF The stability of CANF at high temperatures is necessary for its practical application. Thus, the temperature stability of free CA and CANF was studied.…”

Characterization of 2,3,7,8-tetrachlorodibenzo-p-dioxin biodegradation by extracellular lignin-modifying enzymes from ligninolytic fungus

“…There are three main LME enzyme groups involved in pollutant remediation: lignin peroxidases (LiP), manganese peroxidases (MnP) and laccases. The link between LME and dioxin degradation was shown in P. chrysosporium as this strain (Yadav et al, 2016) produced both LiP and MnP and degrades 2,7-DCDD. During 2,7-DCDD degradation, LiP starts the degradation process by oxidative cleavage of both CeOeC bonds which is followed by further catalysis by both LiP and MnP (Valli et al, 1992).…”

Mechano-chemical and biological energetics of immobilized enzymes onto functionalized polymers and their applications

“…The kinetic parameters of immobilized biocatalyst including turnover number ( K cat ), maximum velocity ( V max ), and Michaelis Menten constant ( K m ), can vary from that of the free biocatalyst [ 65 , 66 ]. However, the immobilization method may affect the kinetic behavior of biocatalyst due to various factors such as limited access to the active center, enzyme conformational changes, and deviation in the microenvironment around the immobilized enzyme etc [ 67 ]. The changes in kinetic parameters such as K m and V max helps to determine the success of the immobilization process.…”