By Katoh S., Yoshida F.
Written by means of popular professors drawing on their event won within the world's so much leading edge biotechnology industry, Japan, this complicated textbook presents a good and complete creation to the most recent advancements within the box. It presents an array of questions & solutions and contours a variety of utilized examples, extending to business purposes with chapters on scientific units and downstream operations in bioprocesses.Useful for college kids learning the basics of biochemical engineering, in addition to for chemical engineers already operating during this important and increasing box.
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Additional resources for Biochemical engineering: A textbook for engineers, chemists, and biologists
KGaA, Weinheim ISBN: 978-3-527-32536-8 28 | 3 Chemical and Biochemical Kinetics where V is the fluid volume (m3) in a reactor, Ni the number of moles of i formed (kmol), and t is the time (s). 1, the suffix i usually designates a reaction product. The rate ri is negative, in case i is a reactant. Several factors, such as temperature, pressure, the concentrations of the reactants, and also the existence of a catalyst, affect the rate of a chemical reaction. In some cases, what appears to be one reaction may in fact involve several reaction steps in series or in parallel, one of which may be rate limiting.
4 Laminar versus Turbulent Flow As mentioned above, two distinct patterns of fluid flow can be identified, namely laminar flow and turbulent flow. Whether a fluid flow becomes laminar or turbulent depends on the value of a dimensionless number called the Reynolds number, (Re). , volumetric flow rate divided by the inside cross-sectional area of the tube), r is the fluid density (M LÀ3), and m is the fluid viscosity (M LÀ1 TÀ1). Under steady conditions, the flow of fluid through a straight round tube is laminar, when (Re) is less than approximately 2300.
2. What is the activity (units cmÀ3) of b-glucosidase in the enzyme solution? 7 An angiotensin-I converting enzyme (ACE) controls blood pressure by catalyzing the hydrolysis of two amino acids (His-Leu) at the C terminus of angiotensin-I to produce a vasoconstrictor, angiotensin-II. The enzyme can also hydrolyze a synthetic substrate, hippuryl-L-histidyl-L-leucine (HHL) to hippuric acid (HA). 7. , Ile-Lys-Tyr) can irreversibly inhibit the ACE activity. 5 mmol lÀ1 of an inhibitory peptide (Ile-Lys-Tyr) are also given in the table.
Biochemical engineering: A textbook for engineers, chemists, and biologists by Katoh S., Yoshida F.