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Biochem

Biochemical engineering concerns the engineering of discovery processes and translation of discoveries in biochemistry and medicine into commercial processes for new biological entities like medicines. It encompasses biology, engineering, mathematics, and business aspects. Bioprocess engineering deals with design and construction of unit processes involving biological organisms or molecules to generate value-added products like fuels, food, and pharmaceuticals. Enzymes are protein catalysts that enable all chemical reactions in living organisms. They function in a mild body-like environment and selectively catalyze specific reactions and substrates. The Michaelis-Menten model describes enzyme kinetics as a reversible binding of substrate and enzyme to form a complex, followed by an irreversible reaction to produce product and regener

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36 views5 pages

Biochem

Biochemical engineering concerns the engineering of discovery processes and translation of discoveries in biochemistry and medicine into commercial processes for new biological entities like medicines. It encompasses biology, engineering, mathematics, and business aspects. Bioprocess engineering deals with design and construction of unit processes involving biological organisms or molecules to generate value-added products like fuels, food, and pharmaceuticals. Enzymes are protein catalysts that enable all chemical reactions in living organisms. They function in a mild body-like environment and selectively catalyze specific reactions and substrates. The Michaelis-Menten model describes enzyme kinetics as a reversible binding of substrate and enzyme to form a complex, followed by an irreversible reaction to produce product and regener

Uploaded by

Neil Briones
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© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Difference between bioprocess from biochemical engineering?

Biochemical engineering concerns the engineering of discovery processes and the translation of
discoveries in Biochemistry and Medicine into commercial processes for new biological entities
such as medicines and therapeutics. It encompasses the biology, engineering, mathematics
and business behind this translation, it is a branch of chemical engineering or biological
engineering that mainly deals with the design and construction of unit processes that involve
biological organisms or molecules while Bioprocess engineering is the alteration or application
of renewable materials to generate value-added products. It encompasses discovery, research,
development and the manufacturing and commercialization of products. Products developed
include: fuels, food, feed, pharmaceuticals, nutraceuticals and a multitude of value-added
biomaterials found in and used by all industries.

What is enzyme?
Enzymes are proteins that have catalytic functions indispensable to maintenance and activity of
life. All chemical reactions occurring in a living organism are dependent on the catalytic actions
of enzymes, and this is why enzymes are called Biotransformation. At present, there are about
4,000 kinds of enzymes whose actions are well known. It functions in a mild environment
similar to the body environment of a living organism, and they support life by synthesizing and
degrading materials that constitute the building blocks of the organism and by creating energy
and also as highly selective catalysis in such a way that they selectivity catalyze specific
reactions (reaction specificity) and specific materials (substrate specificity).

Explain a simple enzyme kinetics using michaelis menten and brigg haldene
The Michaelis-Menten model (1) is the one of the simplest and best-known approaches to
enzyme kinetics. It takes the form of an equation relating reaction velocity to substrate
concentration for a system where a substrateS binds reversibly to an enzyme E to form an
enzyme-substrate complex ES, which then reacts irreversibly to generate a product P and to
regenerate the free enzyme E. This system can be represented schematically as follows:

The Michaelis-Menten equation for this system is:

Here, Vmax represents the maximum velocity achieved by the system, at maximum (saturating)
substrate concentrations. KM (the Michaelis constant; sometimes represented as KS instead) is the
substrate concentration at which the reaction velocity is 50% of the Vmax. [S] is the concentration
of the substrate S.
This is a plot of the Michaelis-Menten equations predicted reaction velocity as a function of
substrate concentration, with the significance of the kinetic parameters Vmax and KM graphically
depicted.

The best derivation of the Michaelis-Menten equation was provided by George Briggs and J.B.S.
Haldane in 1925 (2), and a version of it follows:

For the scheme previously described, kon is the bimolecular association rate constant of enzymesubstrate binding; koff is the unimolecular rate constant of the ES complex dissociating to
regenerate free enzyme and substrate; and kcat is the unimolecular rate constant of
the ES complex dissociating to give free enzyme and product P.

Note that kon has units of concentration-1time-1, and koff and kcat have units of time-1. Also, by
definition the dissociation binding constant of the ES complex, KD is given by koff/kon (and so has
units of concentration).
Once these rate constants have been defined, we can write equations for the rates of change of all
the chemical species in the system:

The last of these equations describing the rate of change of the ES complex is the most
important for our purposes. In most systems, the ES concentration will rapidly approach a
steady-state that is, after an initial burst phase, its concentration will not change appreciably
until a significant amount of substrate has been consumed. This steady-state approximation is
the first important assumption involved in Briggs and Haldanes derivation. This is also the
reason that well-designed experiments measure reaction velocity only in regimes where product
formation is linear with time. As long as we limit ourselves to studying initial reaction velocities,
we can assume that [ES] is constant:

In order to determine the rate of product formation (d[P]/dt = kcat[ES]), we need to rearrange the
equation above to calculate [ES]. We know that the free enzyme concentration [E] is equal to the
total enzyme concentration [ET] minus [ES]. Making these substitutions gives us:

We now make a couple of substitutions to arrive at the familiar form of the Michaelis-Menten
equation. SinceVmax is the reaction velocity at saturating substrate concentration, it is equal
to kcat [ES] when [ES] = [ET]. We also define KM in terms of the rate constants as follows:

Note that [S] here represents the free substrate concentration, but typically is assumed to be close
to the total substrate concentration present in the system. This second assumption is the free
ligand approximation, and is valid as long the total enzyme concentration is well below
the KM of the system. If this condition is not met (for instance, with a very high-affinity
substrate), then the quadratic (or Morrison) equation must be used instead.

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