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Cambridge International AS Level Biology

Answers to end-of-chapter questions

Answers to EOCQs
Chapter 3

1 B;[1]

The mark schemes, suggested answers and


comments that appear in this CD-ROM were written
by the author(s). In examinations, the way marks
would be awarded to answers like these may be
different.

2 D;

Notes about mark schemes

5 straight line drawn from origin at zero to


show steepest gradient of curve;[1]

A or accept indicates an alternative acceptable


answer.
R = reject. This indicates a possible answer that
should be rejected.
; The bold semi-colon indicates the award of 1 mark.
/ This indicates an alternative answer for the same
mark. The alternatives may be separated from the
rest of the answer by commas.
( ) Text in brackets is not required for the mark.
Underlining This is used to indicate essential
word(s) that must be used to get the mark.
AW means alternative wording. It is used to
indicate that a different wording is acceptable
provided the essential meaning is the same, and is
used where students responses are likely to vary
more than usual.
AVP means additional valid point. This means
accept any additional points given by the student
that are not in the mark scheme, provided they are
relevant. But accept only as many additional points
as indicated by the bold semi-colons, e.g. AVP;;
means award a maximum of 2 extra marks.
ORA means or reverse argument and is used when
the same idea could be expressed in the reverse
way. For example: activity increases between pH
2 and pH 5 ORA means accept activity decreases
between pH 5 and pH 2.
max. This indicates the maximum number of marks
that can be given.

[1]

3 D;[1]
4 C;

[1]

6 a
maximum activity / optimum pH, is pH 5;
activity gradually increases between pH 2
and pH 5, and decreases from pH 5 to pH 10;
activity very low at pH 2 and pH 10; AW
[max.2]
b
pH is a measure of the hydrogen ion
concentration;
hydrogen ions are positively charged;
hydrogen ions can interact with the R groups
of amino acids;
affects ionic bonding / affects ionisation of
Rgroups;
affects tertiary structure / affects 3D shape of
enzyme;
therefore substrate may not fit active site
(asprecisely);
[max. 4]
[Total: 6]
7 a
optimum temperature;[1]
b
37C; accept 40C
[1]
c
as temperature increases the kinetic energy
of the molecules increases;
the rate of collision between substrate and,
enzyme / active site, increases;
rate of reaction increases;
[3]
d
the enzyme is gradually being denatured;
when the rate is zero the enzyme is
completely denatured;
ORA enzyme loses tertiary structure;
substrate no longer fits into active site
/ active site loses its (specific) shape so
substrate does not fit;
AVP e.g.hydrogen bonds broken / increased
vibration of enzyme molecule;
[max. 3]

Cambridge International AS and A Level Biology Cambridge University Press 2014

Cambridge International AS Level Biology

Answers to end-of-chapter questions

10

a replication increases reliability; AW[1]
e
the extra energy which must be given to the
substrate;
b
to act as a reference to show what happens if
before it can be converted into the product;
there is no denaturation; AW[1]
[2] c
40C is the optimum temperature for a
[Total: 10]
mammalian enzyme;[1]
enzyme / amylase (molecules) diffuse(s) from
8 a
succinic acid;[1] d
wells into the agar;
b
malonic acid acts as a competitive inhibitor;
enzyme / amylase digests the starch;
it has a similar shape / structure to succinic
to maltose;
acid;
forms rings / halos, of digested starch around
it therefore competes with succinic acid for a
the wells;
place in the active site of the enzyme;[3]
amount of digestion / rate of digestion, is
c i cysteine;[1]
related to degree of denaturation of enzyme /
ii
SH groups form disulfide bridges;
amylase;
[max. 4]
used to determine tertiary structure;
e
the more enzyme / amylase added, the
heavy metal would prevent formation of
greater the amount of digestion of starch
disulfide bridges;
or
want results to be due to differences in
could change shape of active site;
preheating times, not to differences in
heavy metal could affect shape either by
amount of amylase / enzyme; AW[1]
binding directly in the active site, or by
f
binding at another site which then results
in change in shape of the active site;
Time (heated) at 60C / min Diameter of halo / mm
substrate would not be able to fit into
0
24
active site;
[max. 4]
19
1
iii
(non-competitive) irreversible;[1]
[Total: 10]
10
5
9 a
carry out Benedicts test on solutions A, B
6
10
and C;
a positive result / brick-red precipitate will be
0
30
seen, with the glucose solution;
table drawn with ruled lines for border and
heat separate samples of the two remaining
to separate columns and headings (ideally
solutions, in boiling water bath / to high
ruled lines between rows, but not essential
temperature (e.g. 80C), for suitable time / at
for mark);
least two minutes (enzyme will be denatured);
correct headings to columns with units;
for each heated solution, mix it with an
first column is independent variable (Time
unheated sample of the other solution;
heated at 60C);
leave several minutes / suitable time (for
correct measurements of halos;[4]
reaction to take place);
g
measure the four halos and calculate the
carry out Benedicts test on the two tubes;
mean;[1]
only one will give a positive result (due to
(any anomalous results should be ignored)
presence of maltose) and this will be the one
which contained the unheated enzyme;
Accept alternative wording for all steps in
the procedure, provided the same logical
sequence is described
[max. 6]
b
hydrolysis;[1]
[Total: 7]
Cambridge International AS and A Level Biology Cambridge University Press 2014

Cambridge International AS Level Biology

Answers to end-of-chapter questions

h 24

20

Diameter /mm

16

12

10

12

14

16

18

20

22

24

26

28

30

Time at 60C /minutes

x-axis (horizontal axis) is labelled Time


(heated) at 60C, y-axis (vertical axis) is
labelled Diameter;
units given on axes, min / minutes and mm;
regular intervals on both axes (check that
0, 1, 5, 10, 30 are not regularly spaced on
x-axis);
points plotted accurately;
points joined with straight lines or
smoothcurve;[5]
i
enzyme was completely denatured after
30minutes;
rate of denaturation was rapid at first and
then gradually slowed down;
data quoted;
enzyme loses tertiary structure;
substrate no longer fits into active site
/ active site loses its (specific) shape so
substrate does not fit;
AVP e.g. hydrogen bonds broken / increased
vibration of enzyme molecule;
[max. 4]
j
heat samples of mammalian, fungal and
bacterial amylases at different temperatures;
suitable range, e.g. between 40C and 120C;

40C is a control (for reference to find out size


of halo with no denaturation);
at least five temperatures, e.g. 40, 60, 80, 100,
120C;
heat for suitable length of time (e.g. one
hour, at least ten min);
cool to room temp / 40C, add equal volumes
to wells in starchagar plates, replicate wells
in each plate (e.g. four), leave 24 hours,
test for starch, measure diameters of halos;
[max.5]
Background information: amylase enzymes
from the bacterium Bacillus licheniformis and
the fungus Aspergillus have been developed by
biotechnology companies for use in industrial
processes. For example, a bacterial amylase
that functions in the range 90110C has
been developed and is used in beer brewing
and other processes, and a fungal amylase
that operates in the range 5060C is used for
pastry baking and maltose syrup production.
k
pH;
substrate concentration;
enzyme concentration;[3]
[Total: 30]

Cambridge International AS and A Level Biology Cambridge University Press 2014

Cambridge International AS Level Biology

Answers to end-of-chapter questions

11 a see Figure 3.14b. Award 1 mark for each


correct label;;;[3]
b
inhibitor A had no effect on Vmax;
and increased Km;[2]
c
inhibitor B decreased Vmax;
and had no effect on Km;[2]
d
inhibitor A is competitive, B is noncompetitive;
A is competitive because:
it increased Km / did not affect Vmax;
decreased the affinity of the enzyme for its
substrate;
the substrate is competing with the inhibitor
for the active site;
the inhibition is overcome by increasing
substrate concentration;
[max. 4]
Or
Alternative ways of explaining the same
marking points;
B is non-competitive because:
it did not affect Km/decreased Vmax;
did not affect the affinity of the enzyme for its
substrate;
the substrate is not competing with the
inhibitor for the active site;
the inhibition cannot be overcome by
increasing substrate concentration;
e i Z;[1]
ii
Y;[1]
iii
X;[1]
Reasons:
Accept any valid points up to a maximum of
2 marks for each inhibitor, for example:
ii
the lines Y and Z cross the y-axis at the
same point, which is 1/Vmax;
therefore Vmax is the same for both;
line Y meets the x-axis at a less negative
value than line Z;
therefore Km is increased;
[max. 2]
iii
the lines X and Z cross the y-axis at the
same point, (which is 1/Km );
therefore both have the same Km;
line X crosses the y-axis higher than line Z,
so 1/Vmax has a higher value;
therefore Vmax has a lower value; [max. 2]
[Total: 18]
Cambridge International AS and A Level Biology Cambridge University Press 2014

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