UNIVERSITY OF ALGARVE

HIGHER INSTITUTE OF ENGENEERING

MASTER IN FOOD TECHNOLOGY
ENZYMOLOGY
1 SEMESTER – 1ST YEAR - 2020/2021
ST

Name: ______________________________________________________ Nº : _________

Acessment: ____________________ Teacher's signature: __________________________

EXAM – 03-02-2021

1. Enzymes are globular proteins that act in the most varied reactions. Some factors can affect
the activity of these substances, changing the rate of a reaction. Regarding these factors,
indicate the following sentences, true or false, justifying them if they are marked as false.
a) Temperature actively influences enzyme activity, causing the enzyme reaction to
accelerate.
b) pH plays an important role in enzyme activity, and its variation causes little change in the
functioning of enzymes.
c) Very high temperatures can cause the interruption of enzyme activity, as it can cause
denaturation of the enzyme.
d) Most enzymes have an optimum pH around 7.

2. What relative values of KM and kcat would describe an enzyme with high catalytic
efficiency?

a) Low KM and high kcat.

b) High KM and high kcat.
c) High KM and low kcat.
d) Low KM and low kcat.

3. The 'X' molecule is an enzyme inhibitor that reversibly binds to an enzyme at a site that is
distinct from its active center. The 'X' molecule should not be what kind of inhibitor?
a) Competitive inhibitor
b) Non-competitive inhibitor
c) Anti-competitive inhibitor
d) Mixed inhibitor
4. Describe how pH and temperature affect enzyme denaturation.

5. State the main methods of immobilizing enzymes.

6. What is the significance of the KM catalytic constant? What units are measured.

7. Explain the process of action of amylases in bakery products and mention the benefits of
their use.

8. What are the enzymatic coagulation phases of milk? Describe what happens in each of
these phases.
8.1 What characteristics should a good milk coagulating enzyme have?
8.2 What do these characteristics mean?
8.3 What inconveniences can arise in the cheese making process, when using an enzyme with
high KM?

9. Suppose that the data shown below are obtained for an enzyme-catalyzed reaction in the
presence and absence of inhibitor Y.

V (mol.L-1.min-1).
[S] mM Sem inibidor Com inibidor 0.3 mM
0.2 5.0 2.0
0.4 7.5 3.0
0.8 10.0 4.0
1.0 10.7 4.3
2.0 12.5 5.0
4.0 13.6 5.5

9.1 Using Lineweaver Burk representation of the data, determine the inhibition type that
has occurred. Present the graph.
9.2 Calculate Vmax and KM.
9.3 Calculate the inhibitor constant KI for compound Y, when the final concentration of
Y in the reaction mixture was 0.3 mM.
9.4 Does inhibitor Y combine with E, with ES, or with both? Explain.