Biochemical engineering: A textbook for engineers, chemists, by Katoh S., Yoshida F.

By Katoh S., Yoshida F.

Written through popular professors drawing on their event received within the world's so much cutting edge biotechnology industry, Japan, this complicated textbook offers a great and accomplished creation to the newest advancements within the box. It presents an array of questions & solutions and lines a variety of utilized examples, extending to commercial functions with chapters on scientific units and downstream operations in bioprocesses.Useful for college students 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

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4. Calculate the second-order rate constant for this reaction, using the integration method. 001 1/s at 80 1C. Estimate the half-life t1/2 of this enzyme at 80 1C. 6. 83 1. Calculate the initial rate of the enzyme reaction. 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.

5 Temperature gradient in turbulent heat transfer from solid to fluid. For heat transfer q ¼ Àða þ EH Þdðcp rtÞ=dy ð2:13Þ For mass transfer JA ¼ ÀðDAB þ ED ÞðdCA =dyÞ ð2:14Þ For momentum transfer t ¼ Àðv þ EV ÞdðurÞ=dy ð2:15Þ In the above equations, EH, ED, and EV are eddy thermal diffusivity, eddy diffusivity, and eddy kinematic viscosity, respectively, all having the same dimensions (L2 TÀ1). It should be noted that these are not properties of fluid or system, because their values vary with the intensity of turbulence which depends on flow velocity, geometry of flow channel, and other factors.

8 The enzyme invertase catalyzes the hydrolysis of sucrose to glucose and fructose. The rate of this enzymatic reaction decreases at higher substrate concentrations. 8. 216 1. 42. E þ S$ES ES þ S$ES2 kÀ1 =k1 ¼ Km kÀi =ki ¼ KI ES ! E þ P 2. Assuming that the values of Km and KI are equal, determine the value. L. and Altman, C. (1963) J. Phys. , 60, 1375. 2 Michaelis, L. L. (1913) Biochem. , 49, 333. E. S. (1925) Biochem. , 19, 338. 4 Lineweaver, H. and Burk, D. (1934) J. Am. Chem. , 56, 658. , Kokowsky, N.

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