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Question Answer Marks AO Element Notes Guidance

1 protein ; 3
catalysts ;
speed up ;

2(a)(i) protease activity, similar/ AW, 3 max [3]

on both sites;
all enzyme activity is, greater/
better/ faster, in site A;
cellulase activity on site A
greater than protease activity on
site A;
cellulase activity, higher on site
A, than site B/ ORA;
cellulase and protease activity
on site B similar;
use of data with units to support do not award data
any of these marking points; quote unqualified
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Question Answer Marks AO Element Notes Guidance

2(a)(ii) pH/ water content, no effect on 3 max [3]

protease activity;
cellulase more active, at higher
pH/ less acidic environment;
cellulase more active, at lower
soil moisture;
ref to optimum pH of, protease/
cellulase/ enzymes;
low pH may denature
cellulase;
idea of different leaf
composition;
size of leaves/ surface area/
species of leaf;
different stage of
decomposition;

3(a)(i) volume of, oxygen/ gas, 3 max [3]

increases (with time);
levels off/ reaches a plateau/
I 'reaction stops'
AW;
increases rapidly at start and
then slows down;
3
use of data; e.g. levels off at 6.2cm
of oxygen at 90
seconds
data quotes must have
units
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Question Answer Marks AO Element Notes Guidance

3(a)(ii) substrate/ hydrogen peroxide/ 3 max [3] A answers in the

reactant/ AW, fits into context of catalase
enzyme;
I 'speeds up the
active site; reaction'
shape is, complementary/ R if shape is the
AW; same
any reference to lock and key;
product(s)/ oxygen and water, A product and enzyme
formed and leaves the separate e.g. enzyme
enzyme; can work again/
enzyme not used up/
AVP;
enzyme is not changed
during reaction/ lowers
activation energy

4 lock and key mechanism; 3 max [3]

substrate fits into enzyme;
(shape of) substrate is
complementary to, enzyme /
active site;
ref to active site;
substrate breaks/ product(s)
forms/ product(s) leaves
enzyme;
enzyme, free for next reactions/
not used up/ remains
unchanged;
AVP; e.g. lowers activation
energy
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Question Answer Marks AO Element Notes Guidance

5(a)(i) temperature/ pH/ concentration 1 AO1

of substrate/ surface area of
substrate;
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Question Answer Marks AO Element Notes Guidance

5(a)(ii) for temperature: 2 AO1 max [2]

idea of increase in temperature
increases rate/ AW;
enzyme has an optimum
temperature (at which it works
fastest);
at high temperatures enzyme,
stops working/ is denatured;
at low temperatures enzyme,
slows down/ becomes
inactive;
OR
for pH:
extremes of pH reduce rate of
reaction/AW;
extremes of pH denatures
enzyme/ AW;
enzyme has an optimum pH at
which it works fastest;
OR
for concentration/ area of
substrate:
higher concentration/ increase
(surface) area, increases rate of
reaction;
which results in more
collisions;
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Question Answer Marks AO Element Notes Guidance

until all active sites are being

used;

6(a) a substance which, speeds up/ 2 AO1

alters the rate of, a (chemical)
reaction;
not changed/ not used up, by the
reaction;

6(b) proteins; 1 AO1

7(a) biological/ made by cells; 2 AO1 max [2]

catalyst/ speeds up rate of a
reaction;
made of protein;
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Question Answer Marks AO Element Notes Guidance

7(b) tubes 1 and 3 - the effect of 6 AO3 max [6]

pH
1 lyzosyme is active in, 1/ pH
4.0/ acid;
2 cell wall, broken down/
digested/ destroyed in tube 1;
3 no (bacterial) growth in tube
1;
tubes 1 and 4 - the effect of
type of bacteria
4 lysozyme, destroys / AW,
bacteria , A/ in tube 1;
5 lysozyme does not, destroy /
AW, bacteria , B/ in tube 4;
6 ref to specificity to bacteria A/
bacteria B is resistant; ignore
bacteria are immune
7 idea that nothing in (cell wall
of) bacteria B for lysozyme to
digest;
tubes 1 and 2 - the effect of
boiling
8 lysozyme denatured (by
boiling);
9 lysozyme not, active;
10 idea that tube 2 is a control
to show that lysozyme is
responsible for no growth in tube
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Question Answer Marks AO Element Notes Guidance

1;

8(a) candidates have filled in 3

temperatures (lowest to
highest);
times are transferred in correct
sequence 0—20;
colour of indicator recorded
correctly from the diagram of the
students' results in all
columns;

8(b)(i) lipase works best in alkaline 1

conditions/ provides suitable pH
for lipase;

8(b)(ii) idea that both tubes reach the 1

experimental temperature;

8(b)(iii) fatty acids produced by the 2

break down of fat;
(acids) lower pH (causing colour
change);

8(b)(iv) stays blue/ no colour change; 2

enzyme doesn't react/
denatured/ AW;
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Question Answer Marks AO Element Notes Guidance

8(b)(v) anomalous 21°C, for 10 min; 2

reason: idea that the colour
changes are not in the expected
order;

8(c) 2 x 2 of: 4
V: enzyme concentration;
C: same source/ concentration
of enzyme/ lipase used in all
tubes;
V: substrate concentration;
C: same source of milk/ same
type of milk/ or named type;
V: indicator;
C: same concentration/ volume
added/ comparison of colour
with chart or meter;
V: timing length of reaction;
C: minute intervals precisely
using timing device;

8(d) idea of more temperatures/ a 2 max [2]

bigger range of temperatures;
idea of smaller/ uniform intervals
between the temperatures;
example of a better way of
measuring pH;
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Question Answer Marks AO Element Notes Guidance

[Total: 49]