Catalysts are easily deactivated by coking while enzymes are inhibited as active sites are occupied. There are 3 types of enzyme inhibitions (substrate, product and mixed). The main questions would be, how inhibition interact with the nature or structure of enzymes that cause reduction of enzyme's activities?
Enzyme based on its nature specifically act as biocatalysts with very define substrate form enzyme-substrate complex. If any substances with similar group show up as active material get special interaction with enzyme; then it may compete with substrate. Since the reaction is retarded by newly interference molecule known as inhibitor.
As inhibition is retarding the rate of enzymatic reaction, we can observe even inhibition is affected on rate model. For instance, the kinetics of enzymatic reaction of disaccharides such as lactose is affected by β-galactosidase concentration. The reaction may be inhibited with high product concentration. The projected rate is:
V=(Vmax.S)/[Km(1+ P/Ki)+S]
where V is the rate and Vmax is maximum specific rate, S stands for substrate, P for product and Ki is coefficient for inhibition term. For easy recovery of enzyme from milk, the enzyme solution can be entrapped with nitro-cellulose membrane with mesh size of 30 micrometer (microcapsules).
The conentration of enzyme and product and also temperature play a role.
I have one question, how polysaccharide get conerting to oligosaccharide by enzymatic method, and what is the kinetic of this reaction.
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