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 2 D; [1]

comments that appear in this CD-ROM were written
by the author(s). In examinations, the way marks 3 D;[1]
would be awarded to answers like these may be
different. 4 C; [1]

Notes about mark schemes
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.
5 straight line drawn from origin at zero to
show steepest gradient of curve;[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
R groups;
affects tertiary structure / affects 3D shape of
enzyme;
therefore substrate may not fit active site
(as precisely); [max. 4]
[Total: 6]

AVP means ‘additional valid point’. This means 7 a

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.
optimum temperature;[1]
b 37 °C; accept 40 °C [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
e the extra energy which must be given to the
substrate;
before it can be converted into the product;
[2] c 40 °C is the optimum temperature for a
[Total: 10]
8 a succinic acid;[1] d enzyme / amylase (molecules) diffuse(s) from
b malonic acid acts as a competitive inhibitor;
it has a similar shape / structure to succinic
acid;
it therefore competes with succinic acid for a
place in the active site of the enzyme;[3]
c i cysteine;[1]
ii –SH groups form disulfide bridges;
used to determine tertiary structure;
heavy metal would prevent formation of
disulfide bridges;
could change shape of active site;
heavy metal could affect shape either by
binding directly in the active site, or by
binding at another site which then results
in change in shape of the active site;
substrate would not be able to fit into
active site; [max. 4]
iii (non-competitive) irreversible;[1]
[Total: 10]
9 a carry out Benedict’s test on solutions A, B
and C;
a positive result / brick-red precipitate will be
seen, with the glucose solution;
heat separate samples of the two remaining
solutions, in boiling water bath / to high
temperature (e.g. 80 °C), for suitable time / at
least two minutes (enzyme will be denatured);
for each heated solution, mix it with an
unheated sample of the other solution;
leave several minutes / suitable time (for
reaction to take place);
carry out Benedict’s test on the two tubes;
only one will give a positive result (due to
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
Answers to end-of-chapter questions
10
a replication increases reliability; AW[1]
b to act as a reference to show what happens if
there is no denaturation; AW[1]
mammalian enzyme;[1]
wells into the agar;
enzyme / amylase digests the starch;
to maltose;
forms rings / halos, of digested starch around
the wells;
amount of digestion / rate of digestion, is
related to degree of denaturation of enzyme /
amylase; [max. 4]
e the more enzyme / amylase added, the
greater the amount of digestion of starch
or
want results to be due to differences in
preheating times, not to differences in
amount of amylase / enzyme; AW[1]
f
Time (heated) at 60 °C / min Diameter of halo / mm
0 24
1 19
5 10
10 6
30 0
table drawn with ruled lines for border and
to separate columns and headings (ideally
ruled lines between rows, but not essential
for mark);
correct headings to columns with units;
first column is independent variable (Time
heated at 60 °C);
correct measurements of halos;[4]
g measure the four halos and calculate the
mean;[1]
(any anomalous results should be ignored)
 Cambridge International AS Level Biology Answers to end-of-chapter questions

h 24

20

16
Diameter /mm

12

0
2 4 6 8 10 12 14 16 18 20 22 24 26 28 30
Time at 60˚C /minutes

x-axis (horizontal axis) is labelled ‘Time
(heated) at 60 °C’, 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
smooth curve;[5]
i
enzyme was completely denatured after
30 minutes;
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 40 °C and 120 °C;
40 °C is a control (for reference to find out size
of halo with no denaturation);
at least five temperatures, e.g. 40, 60, 80, 100,
120 °C;
heat for suitable length of time (e.g. one
hour, at least ten min);
cool to room temp / 40 °C, add equal volumes
to wells in starch–agar 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 90–110 °C has
been developed and is used in beer brewing
and other processes, and a fungal amylase
that operates in the range 50–60 °C 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 non-
competitive;
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