CAMBRIDGE INTERNATIONAL AS & A LEVEL BIOLOGY: COURSEBOOK

Exam-style questions and sample answers have been written by the authors. In examinations, the way marks are awarded
may be different.

Coursebook answers
Chapter 3
Exam-style questions
The mark schemes, suggested answers and 1 C ; [1]
comments that appear here were written by the 2 D ; [1]
author(s). In examinations, the way marks would
be awarded to answers like these may be different. 3 D ; [1]
4 B ; [1]
Notes about mark schemes  5 C ; [1]
A or accept indicates an alternative acceptable
6 straight line drawn from origin at zero to
answer.
show steepest gradient of curve ; [1]
R = reject. This indicates a possible answer that
7 a maximum activity / optimum pH, is pH
should be rejected.
5.5 ;
; The bold semicolon indicates the award of
activity gradually increases between pH 2
1 mark.
and pH 5.5, and decreases from pH 5.5 to
/ This indicates an alternative answer for the same pH 10 ; activity very low at pH 2 and pH
mark. The alternatives may be separated from the 10 ; AW [max. 2]
rest of the answer by commas.
b pH is a measure of the hydrogen ion
( ) Text in brackets is not required for the mark. concentration ;
Underlining This is used to indicate essential hydrogen ions are positively charged ;
word(s) that must be used to get the mark.
hydrogen ions can interact with the R
AW means ‘alternative wording’. It is used to groups of amino acids ;
indicate that a different wording is acceptable
affects ionic bonding / affects ionisation
provided the essential meaning is the same, and is
of R groups ;
used where students’ responses are likely to vary
more than usual. affects tertiary structure / affects 3D shape
of enzyme ;
AVP means ‘additional valid point’. This means
accept any additional points given by the student therefore substrate may not fit active
that are not in the mark scheme, provided they site (as precisely) ; [max. 4]
are relevant. But accept only as many additional  [Total: 6] 
points as indicated by the bold semicolons, e.g.
AVP ; ; means award a maximum of 2 extra marks. 8 a optimum temperature ; [1]

ORA means ‘or reverse argument’ and is used
when the same idea could be expressed in the
reverse way. For example: ‘activity increases
between pH2 and pH5 ORA’ means accept
‘activity decreases between pH5 and pH2’.
max. This indicates the maximum number of
marks that can be given.
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]

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 CAMBRIDGE INTERNATIONAL AS & A LEVEL BIOLOGY: COURSEBOOK

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 ;
 VP e.g. hydrogen bonds broken /
A the procedure, provided the same logical
increased vibration of enzyme molecule ;
 [max. 3]
e the extra energy which must be given to
the substrate ;
before it can be converted into the product ;
 [2]
 [Total: 10]
9 a succinic acid ;
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 ;
ii  – SH groups form disulfide bridges ;
   used to determine tertiary structure ;
  heavy metal would prevent formation
of disulfide bridges ;   greater the amount of digestion of starch
  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]
 [Total: 9]
10 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

sequence is described [max. 6]
b hydrolysis ; [1]
 [Total: 7]
11 a replication increases reliability ; AW [1]
b to act as a reference to show what
happens if there is no denaturation ;
AW [1]
[1] c 40 °C is (close to) the optimum
temperature for a mammalian enzyme ; [1]
d enzyme / amylase (molecules) diffuse(s)
from wells into the agar ;
enzyme / amylase digests the starch ;
to maltose ; 
forms rings / halos, of digested starch
around the wells ;
[1]
amount of digestion / rate of digestion,
is related to degree of denaturation of
enzyme / amylase ; [max. 4]
e the more enzyme / amylase added, the
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 Diameter of
60 °C / min halo / mm
0 24
1 19
5 10
10 6
30 0

table drawn with lines for border and to
separate columns and headings (ideally
ruled lines and lines between rows, but not
essential for mark) ;
correct headings to columns with units ;

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 CAMBRIDGE INTERNATIONAL AS & A LEVEL BIOLOGY: COURSEBOOK

if this is the rule taught, first column is
independent variable (Time heated at
60 °C) ;
correct measurements of halos ;
g measure the four halos and calculate
the mean ;
(any anomalous results should be ignored)
h 100, 120 °C ;
24
j heat samples of mammalian, fungal and
bacterial amylases at different temperatures ;
suitable range, e.g. between 40 °C and
[4] 120 °C ;
40 °C is a control (for reference to find out
[1] size of halo with no denaturation) ;
at least five temperatures, e.g. 40, 60, 80,
heat for suitable length of time (e.g. one
hour, at least ten minutes) ;

20
cool to room temp / 40 °C, add equal
volumes to wells in starch–agar plates,
replicate wells in each plate (e.g. four),
16
Diameter / mm

leave 24 hours, test for starch, measure

diameters of halos ; [max. 5]
12
 ackground information: amylase enzymes
B
8 from the bacterium Bacillus licheniformis
and the fungus Aspergillus have been
4 developed by biotechnology companies for
use in industrial processes. For example,
0 a bacterial amylase that functions in the
2 4 6 8 10 12 14 16 18 20 22 24 26 28 30 range 90–110 °C has been developed and is
Time at 60˚C / minutes used in beer brewing and other processes,
and a fungal amylase that operates in the
x-axis (horizontal axis) is labelled ‘Time range 50–60 °C is used for pastry baking
(heated) at 60 °C’, y-axis (vertical axis) is and maltose syrup production.
labelled ‘Diameter’ (if the rule IV for the
x-axis, DV for the y-axis is taught) ; k pH ; 

units given on axes, min / minutes and substrate concentration ; 

mm; regular intervals on both axes (check enzyme concentration ; [3]
that 0, 1, 5, 10, 30 are not regularly spaced  [Total: 30]
on x-axis) ;
12 a 
see Figure 3.13. Award 1 mark for each
points plotted accurately ;  correct label ; ; ; [3]
points joined with straight lines or b inhibitor A had no effect on Vmax ; and
smooth curve ; [5] increased Km ; [2]
i enzyme was completely denatured after c inhibitor B decreased Vmax ; and had
30 minutes ;  no effect on Km ; [2]
rate of denaturation was rapid at first and d inhibitor A is competitive, B is non-
then gradually slowed down ; competitive ;
data quoted ;  A is competitive because:
enzyme loses tertiary structure ;  it increased Km / did not affect Vmax ;
substrate no longer fits into active site / decreased the affinity of the enzyme for its
active site loses its (specific) shape so substrate ;
substrate does not fit ; the substrate is competing with the
 VP e.g. hydrogen bonds broken /
A inhibitor for the active site ;
increased vibration of enzyme molecule ; the inhibition is overcome by increasing
 [max. 4] substrate concentration ; [max. 4]

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 CAMBRIDGE INTERNATIONAL AS & A LEVEL BIOLOGY: COURSEBOOK

or 
Alternative ways of explaining the same
marking points:
B is non-competitive because: 
it did not affect Km/decreased Vmax ;
it 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 ;
 [Total: 11]

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