ADAMSON UNIVERSITY

COLLEGE OF ENGINEERING
CHEMICAL ENGINEERING DEPARTMENT

BIOCHEMICAL ENGINEERING

FINAL REQUIREMENT

Submitted By:

Bernales, Candice Gareth P.

Gabinete, Aljomarie

Gonzalgo, Leerra Maurreen Z.

Humarang, Jelain A.

Mateo, Mizzrah

Submitted To:

Engr. Rainier G. Gomez

Date Submitted:

October 21, 2016

1. An enzyme is assayed at an initial substrate concentration of 2 x 10​-5​ M. In 6 minutes,
half of the substrate is used. The K​m​ for the substrate is 2 x 10​-3​ M. The value of k in
minute is:

a. 0.42
b. 0.093
c. 0.115
d. 6.693

2. Given the enzyme with a Km = 5m M and Vmax = 15 m mol/min. If [S] = 20 m M,

which of the following will be true?

a. A 100% increase of Vmax would increase velocity by 100%

b. A 10% decrease in Km would increase velocity
c. Both (a) and (b)
d. A 10 % increase in Vmax would decrease velocity 20 fold

3. Which of the following statements is true for enzymatically catalyzed reaction?

a. The activation energy of the reaction is lowered so that a fewer substrate

molecules can overcome it
b. Additional substrate molecules are energized to overcome the activation energy of
the reaction
c. The activation energy of the reaction is increased, thus decreasing the likelihood
that any substrate molecules will overcome it
d. The activation energy of the reaction is lowered so that a larger proportion of
the substrate qualifies to overcome it

4. Non-competitive inhibitor of an enzyme catalyzed reaction

a. can increase reaction velocity in rare cases

b. binds to Michaelis complex
c. decreases Vmax
d. Both(b) and (c)

5. The plot commonly used for determining the value of V​max​ is

 a. Lineweaver Burk Plot
b. Langmuir plot
c. Eadie-Hofstee plot
d. All of the above

6. A noncompetitive inhibitor of an enzyme-catalyzed reaction

a. increases ​K​M​ and increases V​max

b. increases ​K​M​ and reduces V​max
c. reduces ​K​M​ and increases V​max
d. ​ and reduces V​max
reduces ​KM​

[S] V, no inhibitor V, with Inhibitor

(mM) (mmol/min) (mmol/min)
4.5 6.78 4.58
6.0 9.72 7.5
7.5 11.5 8.56
9.0 12.23 9.12

10.5 15.94 9.88

7. Draw a Lineweaver-Burk Plots for an enzyme with the following data:
 What are the Km and Vmax values for the inhibited and uninhibited enzymes? Is the
inhibitor competitive, non-competitive or uncompetitive?

The growth rate of

E. coli
can be expressed by monod kinetics with the parameters of
µmax = 0.935 hr
-1
and k
s
= 0.71 g/L. Assume that the cell yield Y
x/s
is 0.6 g dry cells per g
substrate. If Cx
0
is 1 g/L and Cs = 10 g/L when the cells start to grow exponentially, at t
0
=
0, show how ln Cx, Cx, Cs, dln Cx/dt and dCx/dt, change with respect to time.
The growth rate of
E. coli
can be expressed by monod kinetics with the parameters of
µmax = 0.935 hr
-1
and k
s
= 0.71 g/L. Assume that the cell yield Y
x/s
is 0.6 g dry cells per g
substrate. If Cx
0
is 1 g/L and Cs = 10 g/L when the cells start to grow exponentially, at t
0
=
0, show how ln Cx, Cx, Cs, dln Cx/dt and dCx/dt, change with respect to time.
The growth rate of
E. coli
can be expressed by monod kinetics with the parameters of
µmax = 0.935 hr
-1
and k
s
= 0.71 g/L. Assume that the cell yield Y
x/s
is 0.6 g dry cells per g
substrate. If Cx
0
is 1 g/L and Cs = 10 g/L when the cells start to grow exponentially, at t
0
=
0, show how ln Cx, Cx, Cs, dln Cx/dt and dCx/dt, change with respect to time.
8. The growth rate of ​S. cerevisiae is expressed in monod kinetics with the parameters of
µmax = 0.894 hr-1 and ks = 0.65 g/L. Assume that the cell yield Yx/s is 0.6 g dry cells
per g substrate. If C​x0 is 1 g/L and C​s = 10 g/L when the cells start to grow exponentially,
at t​0​ = 0, show how ln C​x​, C​x​, C​s​, d(ln C​x​)/dt and d(C​x​)/dt, change with respect to time.