Effect of Enzyme Concen

7/28/2019 Effect of Enzyme Concen

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BIOLOGY LAB REPORT

TITLE : THE EFFECT OF ENZYME CONCENTRATION ON

RATE OF REACTION

PREPARED BY :

I/C NUMBER :

STUDENT ID :

GROUP :

LECTURERS NAME

PRACTICAL DATE :

SUBMISSION DATE :


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OBJECTIVE

To investigate the effect of enzyme concentration on the rate of reaction.

Introduction

ENZYME (2)

Enzyme is a protein made up biological catalyst which speeds up the rate of reaction without

changing the product and not altered at the end of the reaction .There are two type of reaction

namely anabolic ( formation of substance from two or more substrate molecule ) and catabolic

(breakdown of substance into two or more products). Combination of anabolic and catabolic reaction

is known as metabolic reaction which involves both reaction. Most enzymes are globular protein .

Enzyme can be divided in two general structure : simple enzyme ( an enzyme that composed of only

amino acid chains) and conjugated enzyme (holoenzyme that has cofactor in addition to apoenzyme).

Enzyme action can be intracellular (within the body cells) or extracellular (outside the body cell).

Basic enzyme mechanism is to form enzyme-substrate complex.

STRUCTURE OF ENZYME(2)

Diagram 1 : Enzyme ribbon structure(1)

Diagram 2 : Enzyme with its active site(1)

Enzymes are complex protein (tertiary or quaternary structure) that made up several polypeptide

chains joined together and held by bonds such as disulphide bond, hydrogen bond, ionic bond and

hydrophobic and hydrophilic interaction which gives the enzyme its precise 3D structure. Enzyme

molecule also has an active site which has a distinctive shape , give enzyme great specificity and

results in catalyzing only one specific reaction. The active site is the most important site in an enzyme

as any alter in the enzyme structure ( denaturation ) will results in inability of catalizing any reaction.


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LOWERING ACTIVATION ENERGY(2)

Enzyme work by lowering activation energy (minimum energy required to initiate a chemical

reaction) that is required at certain reaction to take place.

Diagram 3 : Lowering activation energy by enzyme(1)

Thus by lowering the activation energy, a substrate have no need to achieve transition state before a

product form. This lowers the time taken to produce the product .


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MODEL OF ENZYME ACTION(2)

There are two models that were proposed by scientists. The first on is the lock-and-key model. In this

model, it is said that the active site is exactly complementary to substrate shape and do not change

shape when the substrate molecule come in contact with the active site.

Diagram 4 : Lock-and-key model(1)

The second model that is proposed by scientists is the induced fit model. This model said to be more

reliable because the active site is more flexible and not exactly complementary to the substrates

shape. Thus , when the substrate molecules come into contact with the active site, the enzyme

molecule change shape slightly to fit more closely around the substrate but revert to its shape back

ones the reaction is done.

Diagram 5 : Induced fit model(1)


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ENZYME INHIBITION(2)

Diagram 6 : Two types of inhibition(1)

CATALASE(3)

In this experiment , enzyme catalase used to investigate the effect of enzyme concentration on the

rate of reaction. Catalase is a common and potent enzyme that can be found in almost all living

things. This four polypeptide chain enzyme is used to catalyse the decomposition of hydrogen

peroxide into oxygen gas and water without producing harmful free radicals.

Diagram 7 : 3D structure of catalase(1)


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HYDROGEN PEROXIDE(4)

Hydrogen peroxide (H2O2) is a very pale blue liquid which is slightly more viscous than water. Since it

has high oxidizing power, it is often used as bleach or commonly known as cleaning agent to remove

stains. Hydrogen peroxide also considered as highly reactive oxygen species. Below shows an

equation showing the decomposition of hydrogen peroxide to its constituent substance.

2 H2O2 2 H2O + O2

Caution should be taken when handling with hydrogen peroxide as it is very corrosive.

BUFFER SOLUTION(5)

A buffer solution is an aqueous solution that consists of a mixture of a weak acid and its conjugate

base or weak base and a conjugate acid. It has property that resist the changes in pH when acid or

alkali is added to it. Thus, this ensure that the pH value is maintained throughout the experiment and

is a controlled variable. Two types of buffer solution that is always used in experiments are alkaline

buffer solution which has value more than 7 and acidic buffer solution which has value less than 7.

In this experiment, a buffer solution of pH 6.5 which is a acidic buffer solution is used as it is the

optimum pH value for the decomposition of hydrogen peroxide to its constituent product in the

present of blended potato as the catalase enzyme.


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Problem Statement :

What is the effect of enzyme concentration (catalase) on rate of reaction?

Hypothesis :

The higher the enzyme concentration, the higher the volume of oxygen gas collected ,thus higher the

initial rate of reaction.

Variables :

Types of Variables Ways to control the variables

Manipulated Variable:

Enzyme concentration

(Number of spatula of blended potato )Use different amount of blended potato

(catalase) as in 1 spatula, 2 spatula and 3

spatula.

Responding Variables:

Rate of reaction (cms1)

Volume of oxygen gas produced (due to

decomposition of hydrogen peroxide) until

the reaction over and a tangent drawn at

the graph and the contact point was

calculated using the formula :

Volume of oxygen gas collected (cm)

time (s)

= Rate of reaction (cms1)

Fixed Variables:

pH of the solution

Volume of hydrogen peroxide solution(cm

3

)

Use pH6.5 as the buffer solution

throughout experiment

Use 2.5 cm of hydrogen peroxidethroughout the experiment.


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Apparatus

Test tubes, 250ml beaker, spatula, test tube rack, graduated tube, bung, stopwatch, delivery tube,

droppers, 5ml measuring cylinder and conical flask.

Materials

Water , hydrogen peroxide, blended potato, pH 6,5 buffer solution

Technique used

Volume of oxygen gas evolved due to decomposition of hydrogen peroxide in the present of blended

potato as the enzyme was collected in a graduated tube , fully filled with water before immersed into

a beaker full with water. The volume of oxygen gas collected was measured every 10 seconds for 300

seconds until the reaction finishes by reading the scale of graduated tube.


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Procedure :

1. One spatula of blended potato was taken using spatula and placed into a beaker.

2. 5cm of pH6.5 buffer solution was measured using small measuring cylinder and a

dropper and was transferred into the same beaker.

3. The beaker was swirled to allow the buffer solution and the blended potato to mix

evenly.

4. The mixture was poured into conical flask and was left aside.

5. A 250ml beaker was filled with of water. Then, a graduated tube was completely

filled under running water from pipe. The mouth of graduated tube was covered fully

with thumb to prevent any formation of bubbles and carefully was inverted into the

beaker fill with of water.

6. A delivery tube was connected with its end inserted under the graduated tube

through its mouth.

7. A clean dropper was used to measure 2.5cm of hydrogen peroxide and was placed

into another clean small measuring cylinder. This mixture was then added quickly into

the conical flask containing the mixture of blended potato and buffer solution.

8. The bung of the delivery tube was immediately placed into the mouth of the test tube.

9.

The volume of oxygen gas collected in the graduated tube was observed and recordedfor every 10 seconds until the end of the reaction.

10.Steps 1 until 9 was repeated by replacing 1 spatula of blended potato with two and

three spatula of blended potato.

11.The time taken and volume of oxygen gas collected is tabulated in Table 1.

12.Graph of volume of gas collected against time was plotted for each experiment.

13.Another graph was plotted to show the distinct different in the volume of oxygen gas

produced.14.The initial rate of reaction was calculated from the gradient of the curve and was

tabulated.

15.Another graph of initial rate of reaction against enzyme concentration is plotted.


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RESULTS

DATA COLLECTION

Time (s) Volume of oxygen gas collected for 1 spatula of blended potato (cm)

First reading Second reading Third reading Average reading

0 0.0 0.0 0.0 0.0

30 1.5 1.9 2.0 1.8

60 2.3 3.2 2.9 2.8

90 4.0 3.8 4.2 4.0

120 4,8 5.2 5.0 5.0

150 5.6 6.2 5.6 5.8

180 6.2 6.5 5.9 6.2

210 6.5 5.9 6.8 6.4

240 6.7 6.3 6.2 6.4

270 6.4 6.3 6.4 6.4

300 6.0 6.7 6.5 6.4

Table 1 : Average reading for volume of oxygen collected for 1 spatula of

blended potato against time


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0 0.0 0.0 0.0 0.0

30 2.4 3.2 2.8 2.8

60 6.5 6.8 5.3 6.2

90 8.5 9.0 9.4 9.0

120 11.4 11.2 11.0 11.2

150 13.0 13.7 12.9 13.2

180 14.5 15.0 14.9 14.8

210 15.7 15.9 `15.2 15.6

240 15.8 16.0 16.2 16.0

270 16.0 16.1 16.8 16.3

300 16.2 16.2 16.8 16.4

Table 2 : Average reading for volume of oxygen collected for 2 spatula ofblended potato against time


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0 0.0 0.0 0.0 0.0

30 6.2 6.4 6.3 6.3

60 9.1 9.0 10.1 9.4

90 11.2 12.0 11.0 11.4

120 12.6 12.9 12.9 12.8

150 13.5 13.9 14.0 13.8

180 14.5 14.9 16.5 15.3

210 15.6 16.2 16.8 16.2

240 16.3 16.8 17.3 16.8

270 16.8 17.4 18.3 17.5

300 17.2 17.9 19.8 18.3

Table 3 : Average reading for volume of oxygen collected for 3 spatula ofblended potato against time


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Time against volume of oxygen gas collected for 1 spatula of

blended potato (cm)

0

1

2

3

4

5

6

7

0 30 60 90 120 150 180 210 240 270 300

Graph 2 : Time against volume of oxygen gas collected for 1 spatula of blended potato (cm)

Rate of reaction : = 1.8 cm3

30s

= 0.06 cm3s

-1

olu

eofoxy

encollectedfor1spatulaofblendedpotato

(c

3)

Time (s)


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blended potato (cm)

0

2

4

6

8

10

12

14

16

18

0 30 60 90 120 150 180 210 240 270 300



90s

= 0.09 cm3s

-1

olu

eofoxy

encollectedfor2spatulaofblendedpotato

(c

3)

Time (s)


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blended potato (cm)

0

2

4

6

8

10

12

14

16

18

20

0 30 60 90 120 150 180 210 240 270 300



30s

= 0.21 cm3s

-1

olu

eofoxy

encollectedfor3spatulaofble

ndedpotato

(c

3)

Time (s)


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Time against initial rate of reaction

0

0.05

0.1

0.15

0.2

0.25

0 0.5 1 1.5 2 2.5 3 3.5

Rateof

reaction(cm3s-1

)

Number of spatula of blended potato

Graph 5 : Rate of reaction against time


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Number of spatula of blended

potato (catalase concentration)

Initial rate of reaction (cm3s-1)

1 0.06

2 0.09

3 0.21

Table 4 : Number of spatula of blended potato (catalase concentration) against initial rate of reaction


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DISCUSSION

Analysis of data

An experiment was held to investigate the effect of enzyme concentration on the rate of

reaction. To be more specific, this investigation was held to study the relationship between

concentration of enzyme catalase (number of spatula of blended potato) and the rate of reaction

(decomposition of hydrogen peroxide to produce oxygen gas).

One spatula of blended potato was placed in a beaker and 5cm3

of pH 6.5 buffer was added

and the mixture is swirled. The mixture was then placed into a conical flask. A graduated tube was

filled with water and inserted carefully into a beaker full with water. 2.5cm3

of hydrogen peroxide

solution was added into conical flask using small measuring cylinder and immediately, the graduated

tube was placed over the end of the delivery tube and the volume of oxygen gas collected for every

10 seconds was calculated using stopwatch. The reading was repeated thrice and average reading is

obtained. The results were tabulated and the graphs were drawn. Those steps were repeated using 2

and 3 spatula of blended potato and results obtained were tabulated and graphs were drawn. And

for the last step, the rate of reaction for every enzyme concentration was calculated and another

graph was drawn to show the distinct characteristic of enzyme concentration on the initial rate of

reaction.

The dependant variable is the number of spatula of blended potato which represents catalase

or enzyme concentration. Different amount of blended potato such as increasing number of spatula

of blended potato from one to three was used to observe clearly the effect of different enzyme

concentration on the initial rate of reaction. The independent variable in this experiment is the initial

rate of reaction. This is obtain through simple calculation by dividing the volume of oxygen gas

collected at a contact point on graph by its specific time. The results are precise and valid since the

volume of oxygen gas collected were repeated thrice for every single repeated steps and graphs

were drawn and used to determine the initial rate of reaction. From the graph, it can be concluded

that the higher the enzyme concentration, the higher the initial rate of reaction.


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There are some variables that are kept constant throughout the experiment. It is because the

activity of an enzyme not solely depend on its concentration, but other factors as well. Such variable

is the pH of surrounding. It is kept constant by using a buffer solution at pH6.5. The volume of

hydrogen peroxide solution kept constant by using the same volume throughout the experiment as

volume of substrate also effect enzymatic reaction. Since all of the experiment carried out in the

laboratory, thus the temperature is kept constant at room temperature too.

Graph 1 shows volume of oxygen gas collected for each number of spatulas against time as a

overall to show a distinct difference between one experiment with another. There are three curves

with different colour representing the enzyme concentration for one, two and three spatulas

respectively.

From the overall graph 1 it can be said that increase in enzyme concentration results in

increase of initial reaction. For volume of oxygen gas collected or one spatula of blended potato, it

can be seen that at the beginning of the experiment until 150th

second, the rate of reaction increases

steeply which is indicted by the steep gradient of the curve at the period. It shows that the increase

in rate of reaction is constant during that period of time. The same goes with the graph of two

spatula usage of enzyme ( from beginning until 90th

second) and the graph of three spatula usage of

enzyme (from beginning until 30th

second). At beginning of experiment, the number of hydrogen

peroxide molecule is high, thus the rate of enzymatic reaction not limited by enzyme concentration.

The blended potato catalase enzyme continuously binds with the vacant hydrogen peroxide

molecules and catalyses the substrate, producing oxygen and water.(2)

From 150th

until 210th

second, for the one spatula usage of enzyme , the steepness of the

gradient of the curves decreases. Same goes with the graph of two spatula usage of enzyme ( from

90th

second until 225th

second) and the graph of three spatula usage of enzyme (from 30th

second

until 195th second). This graph trend pictures that for this period of times, less hydrogen peroxide

molecule is decomposed and less oxygen gas is produced and collected .The volume of oxygen

collected is no longer proportional to the enzymes concentration as there is less vacancy of

hydrogen peroxide molecule as quite big amount has been catalysed earlier in the early reaction here

hydrogen peroxide decomposes into oxygen and water.(2)


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Since the amount of hydrogen peroxide molecules left uncatalysed decrease, but there are

more enzyme molecules (part of number of enzyme molecule is not occupied by the substrate in the

active site) , the amount of substrate molecule become limiting factor, thus limiting the rate of

reaction.

A tangent was drawn on the curve of the graphs( graphs 2,3 and 4) to determine the initial

rate of reaction. All three drawn tangents show a positive correlation which indicate the higher the

enzyme concentration the higher the volume oxygen gas produced. It also crease in order from lower

to higher enzyme concentration. The initial rate of reaction is calculated using the formula below ;

Rate of reaction : Volume of oxygen collected at the contact point (cm3)

Time (s)

The initial rate of reaction is represented by the volume of oxygen gas produce divided by the time

which can be concluded as the initial rate of reaction is the gradient of curves tangent.

From table 4, it can be inferred that enzyme concentration of three spatula has the steepest

gradient and highest initial rate of reaction of 0.21 cm

3

s

-1

while the east steep gradient and lowestinitial rate of reaction is at enzyme concentration of one spatula which is 0.06 cm

3s

-1. These

information used to plot graph 5 ( initial rate of reaction against enzyme concentration).in the graph

it can be see that the initial rate of reaction double when the concentration of enzyme doubles.

Biologically, this is because, when enzyme concentration is doubled , amount of enzyme-substrate

complex form also doubles causing double amount of oxygen gas to be collected and thus indicates

double rate of reaction.

It can be seen that from graph 1 , when one spatula of enzyme used, the curve of graph at

210th

second and above become a straight line, indicating zero value of tangent. This shows at this

time, the enzymesubstrate complex is at maximum amount and no active site of enzyme is

available for enzymatic reaction.


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The substrate molecule have to queue up for access to an active site. Any addition of enzyme

molecule number wont alter the reaction, thus no increase in rate of reaction.(2)

As conclusion, it can be concluded that the higher the enzyme concentration, the higher the

initial rate of reaction. When substrate concentration kept constant increase in enzyme

concentration wont increase the rate of reaction.


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Evaluation

Limitation and improvement

Several limitation are found in this experiment. Blended potato in this experiment were prepared

earlier by the laboratory assistant, thus the blended potato had been exposed to air for period of

time before the experiment conducted. The air surrounding oxidized the catalase (blended potato)

therefore reduces the efficiency of enzyme. Exposing blended potato before experiment should be

avoided to get accurate results. Care should be taken by covering mouth of beaker to prevent further

oxidation.

Furthermore, as the spatula is not a measuring apparatus, thus volume of blended potato that is

scooped every time is not the same. The volume and dimension of spatula is not the same and there

is no graduation marks on the spatula. Leveling off the blended potato before transfer or blended

potato should scooped by same person ( human judgement) can be done to get accurate results.

Another limitation is the presence of air bubbles in the graduated tube. Since the experiment were

repeated many time, care is taken when water filled into the graduated tube under running water

but usage of thumb to prevent air bubbles from forming inside not much successful. The presence of

air bubbles in graduated tube gives less accurate reading for the volume of oxygen gas collected due

to decomposition of hydrogen peroxide in the presence of blended potato as catalase. Repeating the

experiment will enable us to get average reading and volume needed can be calculate more

accurately.


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Validity and reability

For ensure the validity of the results, the hydrogen peroxide solution reading in small cylinder and

volume of oxygen in graduated tube was taken with placing eye directly perpendicular to the scale

to prevent any parallax error, thus ensure reading of data results in accurate measurement and

result.

Volume of oxygen gas collected over certain period of time experiment was repeated thrice

for every different enzyme concentration namely 1 spatula of blended potato, 2 spatula of blended

potato and three spatula of blended potato. Obtaining average reading will minimize random errors,

thus ensure the validity and reability of the data.

Extra care was taken when mixture of buffer solution and blended potato were transferred

into conical flask. It is noticed that some of the mixture was smeared on the inner surface of beaker

and was unable to detach itself from the wall. Thus a spatula is used to remove the mixture and

transfer those mixture into the conical flask before proceed to the next step of experiment. This

ensures amount of blended potato and buffer solution used is preserved thus guarantee the validity

and reability of data.

After the mixture of buffer solution and blended potato is poured into the conical flask

containing hydrogen peroxide, it is seen that the bung could not have been close immediately which

results in large amount of oxygen released into air before can be calculated. Thus, the arrangement

of apparatus were made close enough with each other to minimize oxygen gas that released into

surrounding and the bung is closed as fast as could. The repeating of this experiment too help to

obtain more accurate reading thus this ensure the reability and validity of data.


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Safety precaution

In order to avoid any accident or injury during the experiment in laboratory, the

precautionary steps should be taken and applied. Wearing lab coat and a pair of suitable shoes are

compulsory when conducting an experiment in the lab at all times to protect the skin and clothing

from spillage of any chemical substance. This is to ensure that no blended potato or buffer solution

or most importantly hydrogen peroxide is spilled to our skin and clothing as it will stain badly.

Furthermore, the glassware such as beakers and boiling tubes should be handled with full care

because they are fragile. Not only that, caution should applied when handling hydrogen peroxide as

it is corrosive due to its high oxidizing power. If any spillage on the skin or any contact with hydrogen

peroxide solution occur, the skin should be washed under running water immediately to prevent any

injury or defect. When taking measurements form the apparatus, make sure to avoid any human

error such as parallax error. It is very important to take the reading of volume of oxygen collected in

the graduated tube at least three times to get a more accurate, valid and reliable result. Avoid

consuming or tasting any blended potato in experiment because they might be contaminated.

Conclusion

It can be concluded that when the enzyme concentration increases, the initial rate of

enzymatic reaction also increases. The hypothesis is accepted.


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Reference

1. http://www.google.com.my/search?q=enzyme&hl=en&safe=off&biw=1366&bih=681&prmd=

imvnsb&source=lnms&tbm=isch&ei=vK9yTu2HAcrOrQfFrOGyCg&sa=X&oi=mode_link&ct=mo

de&cd=2&sqi=2&ved=0CBcQ_AUoAQ#hl=en&safe=off&tbm=isch&sa=1&q=enzyme+lock+and

+key+diagram+and+induced+fit+model+diagram&oq=enzyme+lock+and+key+diagram+and+i

nduced+fit+model+diagram&aq=f&aqi=&aql=&gs_sm=e&gs_upl=39234l54818l0l55052l34l34l

0l31l31l0l171l437l0.3l3l0&bav=on.2,or.&fp=e4beb283b7067655&biw=1366&bih=681

2. Stoker, H. General, Organic, and Biological Chemistry 7th Edition.

3. http://en.wikipedia.org/wiki/Catalase

4. http://en.wikipedia.org/wiki/Hydrogen_peroxide

5. http://en.wikipedia.org/wiki/Buffer_solution
http://www.google.com.my/search?q=enzyme&hl=en&safe=off&biw=1366&bih=681&prmd=imvnsb&source=lnms&tbm=isch&ei=vK9yTu2HAcrOrQfFrOGyCg&sa=X&oi=mode_link&ct=mode&cd=2&sqi=2&ved=0CBcQ_AUoAQ#hl=en&safe=off&tbm=isch&sa=1&q=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&oq=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&aq=f&aqi=&aql=&gs_sm=e&gs_upl=39234l54818l0l55052l34l34l0l31l31l0l171l437l0.3l3l0&bav=on.2,or.&fp=e4beb283b7067655&biw=1366&bih=681http://www.google.com.my/search?q=enzyme&hl=en&safe=off&biw=1366&bih=681&prmd=imvnsb&source=lnms&tbm=isch&ei=vK9yTu2HAcrOrQfFrOGyCg&sa=X&oi=mode_link&ct=mode&cd=2&sqi=2&ved=0CBcQ_AUoAQ#hl=en&safe=off&tbm=isch&sa=1&q=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&oq=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&aq=f&aqi=&aql=&gs_sm=e&gs_upl=39234l54818l0l55052l34l34l0l31l31l0l171l437l0.3l3l0&bav=on.2,or.&fp=e4beb283b7067655&biw=1366&bih=681http://www.google.com.my/search?q=enzyme&hl=en&safe=off&biw=1366&bih=681&prmd=imvnsb&source=lnms&tbm=isch&ei=vK9yTu2HAcrOrQfFrOGyCg&sa=X&oi=mode_link&ct=mode&cd=2&sqi=2&ved=0CBcQ_AUoAQ#hl=en&safe=off&tbm=isch&sa=1&q=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&oq=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&aq=f&aqi=&aql=&gs_sm=e&gs_upl=39234l54818l0l55052l34l34l0l31l31l0l171l437l0.3l3l0&bav=on.2,or.&fp=e4beb283b7067655&biw=1366&bih=681http://www.google.com.my/search?q=enzyme&hl=en&safe=off&biw=1366&bih=681&prmd=imvnsb&source=lnms&tbm=isch&ei=vK9yTu2HAcrOrQfFrOGyCg&sa=X&oi=mode_link&ct=mode&cd=2&sqi=2&ved=0CBcQ_AUoAQ#hl=en&safe=off&tbm=isch&sa=1&q=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&oq=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&aq=f&aqi=&aql=&gs_sm=e&gs_upl=39234l54818l0l55052l34l34l0l31l31l0l171l437l0.3l3l0&bav=on.2,or.&fp=e4beb283b7067655&biw=1366&bih=681http://www.google.com.my/search?q=enzyme&hl=en&safe=off&biw=1366&bih=681&prmd=imvnsb&source=lnms&tbm=isch&ei=vK9yTu2HAcrOrQfFrOGyCg&sa=X&oi=mode_link&ct=mode&cd=2&sqi=2&ved=0CBcQ_AUoAQ#hl=en&safe=off&tbm=isch&sa=1&q=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&oq=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&aq=f&aqi=&aql=&gs_sm=e&gs_upl=39234l54818l0l55052l34l34l0l31l31l0l171l437l0.3l3l0&bav=on.2,or.&fp=e4beb283b7067655&biw=1366&bih=681http://www.google.com.my/search?q=enzyme&hl=en&safe=off&biw=1366&bih=681&prmd=imvnsb&source=lnms&tbm=isch&ei=vK9yTu2HAcrOrQfFrOGyCg&sa=X&oi=mode_link&ct=mode&cd=2&sqi=2&ved=0CBcQ_AUoAQ#hl=en&safe=off&tbm=isch&sa=1&q=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&oq=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&aq=f&aqi=&aql=&gs_sm=e&gs_upl=39234l54818l0l55052l34l34l0l31l31l0l171l437l0.3l3l0&bav=on.2,or.&fp=e4beb283b7067655&biw=1366&bih=681http://www.google.com.my/search?q=enzyme&hl=en&safe=off&biw=1366&bih=681&prmd=imvnsb&source=lnms&tbm=isch&ei=vK9yTu2HAcrOrQfFrOGyCg&sa=X&oi=mode_link&ct=mode&cd=2&sqi=2&ved=0CBcQ_AUoAQ#hl=en&safe=off&tbm=isch&sa=1&q=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&oq=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&aq=f&aqi=&aql=&gs_sm=e&gs_upl=39234l54818l0l55052l34l34l0l31l31l0l171l437l0.3l3l0&bav=on.2,or.&fp=e4beb283b7067655&biw=1366&bih=681http://www.google.com.my/search?q=enzyme&hl=en&safe=off&biw=1366&bih=681&prmd=imvnsb&source=lnms&tbm=isch&ei=vK9yTu2HAcrOrQfFrOGyCg&sa=X&oi=mode_link&ct=mode&cd=2&sqi=2&ved=0CBcQ_AUoAQ#hl=en&safe=off&tbm=isch&sa=1&q=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&oq=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&aq=f&aqi=&aql=&gs_sm=e&gs_upl=39234l54818l0l55052l34l34l0l31l31l0l171l437l0.3l3l0&bav=on.2,or.&fp=e4beb283b7067655&biw=1366&bih=681http://www.google.com.my/search?q=enzyme&hl=en&safe=off&biw=1366&bih=681&prmd=imvnsb&source=lnms&tbm=isch&ei=vK9yTu2HAcrOrQfFrOGyCg&sa=X&oi=mode_link&ct=mode&cd=2&sqi=2&ved=0CBcQ_AUoAQ#hl=en&safe=off&tbm=isch&sa=1&q=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&oq=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&aq=f&aqi=&aql=&gs_sm=e&gs_upl=39234l54818l0l55052l34l34l0l31l31l0l171l437l0.3l3l0&bav=on.2,or.&fp=e4beb283b7067655&biw=1366&bih=681http://en.wikipedia.org/wiki/Catalasehttp://en.wikipedia.org/wiki/Catalasehttp://en.wikipedia.org/wiki/Hydrogen_peroxidehttp://en.wikipedia.org/wiki/Hydrogen_peroxidehttp://en.wikipedia.org/wiki/Buffer_solutionhttp://en.wikipedia.org/wiki/Buffer_solutionhttp://en.wikipedia.org/wiki/Buffer_solutionhttp://en.wikipedia.org/wiki/Hydrogen_peroxidehttp://en.wikipedia.org/wiki/Catalasehttp://www.google.com.my/search?q=enzyme&hl=en&safe=off&biw=1366&bih=681&prmd=imvnsb&source=lnms&tbm=isch&ei=vK9yTu2HAcrOrQfFrOGyCg&sa=X&oi=mode_link&ct=mode&cd=2&sqi=2&ved=0CBcQ_AUoAQ#hl=en&safe=off&tbm=isch&sa=1&q=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&oq=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&aq=f&aqi=&aql=&gs_sm=e&gs_upl=39234l54818l0l55052l34l34l0l31l31l0l171l437l0.3l3l0&bav=on.2,or.&fp=e4beb283b7067655&biw=1366&bih=681http://www.google.com.my/search?q=enzyme&hl=en&safe=off&biw=1366&bih=681&prmd=imvnsb&source=lnms&tbm=isch&ei=vK9yTu2HAcrOrQfFrOGyCg&sa=X&oi=mode_link&ct=mode&cd=2&sqi=2&ved=0CBcQ_AUoAQ#hl=en&safe=off&tbm=isch&sa=1&q=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&oq=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&aq=f&aqi=&aql=&gs_sm=e&gs_upl=39234l54818l0l55052l34l34l0l31l31l0l171l437l0.3l3l0&bav=on.2,or.&fp=e4beb283b7067655&biw=1366&bih=681http://www.google.com.my/search?q=enzyme&hl=en&safe=off&biw=1366&bih=681&prmd=imvnsb&source=lnms&tbm=isch&ei=vK9yTu2HAcrOrQfFrOGyCg&sa=X&oi=mode_link&ct=mode&cd=2&sqi=2&ved=0CBcQ_AUoAQ#hl=en&safe=off&tbm=isch&sa=1&q=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&oq=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&aq=f&aqi=&aql=&gs_sm=e&gs_upl=39234l54818l0l55052l34l34l0l31l31l0l171l437l0.3l3l0&bav=on.2,or.&fp=e4beb283b7067655&biw=1366&bih=681http://www.google.com.my/search?q=enzyme&hl=en&safe=off&biw=1366&bih=681&prmd=imvnsb&source=lnms&tbm=isch&ei=vK9yTu2HAcrOrQfFrOGyCg&sa=X&oi=mode_link&ct=mode&cd=2&sqi=2&ved=0CBcQ_AUoAQ#hl=en&safe=off&tbm=isch&sa=1&q=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&oq=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&aq=f&aqi=&aql=&gs_sm=e&gs_upl=39234l54818l0l55052l34l34l0l31l31l0l171l437l0.3l3l0&bav=on.2,or.&fp=e4beb283b7067655&biw=1366&bih=681http://www.google.com.my/search?q=enzyme&hl=en&safe=off&biw=1366&bih=681&prmd=imvnsb&source=lnms&tbm=isch&ei=vK9yTu2HAcrOrQfFrOGyCg&sa=X&oi=mode_link&ct=mode&cd=2&sqi=2&ved=0CBcQ_AUoAQ#hl=en&safe=off&tbm=isch&sa=1&q=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&oq=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&aq=f&aqi=&aql=&gs_sm=e&gs_upl=39234l54818l0l55052l34l34l0l31l31l0l171l437l0.3l3l0&bav=on.2,or.&fp=e4beb283b7067655&biw=1366&bih=681http://www.google.com.my/search?q=enzyme&hl=en&safe=off&biw=1366&bih=681&prmd=imvnsb&source=lnms&tbm=isch&ei=vK9yTu2HAcrOrQfFrOGyCg&sa=X&oi=mode_link&ct=mode&cd=2&sqi=2&ved=0CBcQ_AUoAQ#hl=en&safe=off&tbm=isch&sa=1&q=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&oq=enzyme+lock+and+key+diagram+and+induced+fit+model+diagram&aq=f&aqi=&aql=&gs_sm=e&gs_upl=39234l54818l0l55052l34l34l0l31l31l0l171l437l0.3l3l0&bav=on.2,or.&fp=e4beb283b7067655&biw=1366&bih=681

Effect of Enzyme Concen

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