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Enzyme Kinetics and Immobilization Enzyme Kinetics and Immobilization


I. Identification. I. Identification.
Second order Lock-and-key theory Entrapment Second order Lock-and-key theory Entrapment
Third order Michaelis-Menten Briggs-Haldane Third order Michaelis-Menten Briggs-Haldane
Zero Order Cross Linking Adsorption Zero Order Cross Linking Adsorption
Enzymes Enzyme immobilization Enzymes Enzyme immobilization

1.) Biological catalysts that are protein in nature. 1.) The movement of the enzyme in a fixed location is
2.) Original theory to account for the formation of the restricted by attaching them to an insoluble support
enzyme-substrate complex. medium or enclosed by the support medium which is also
3.) In this approach that the product releasing step is much known as the carrier. - enzyme immobilization
slower than the reversible reaction and the slow step 2.) This method of enzyme immobilization has a major
determines the rate while the other is at equilibrium. advantage in the fact that there is no chemical modification
4.) This is also known as the pseudo-steady-state of the enzyme. - entrapment
assumption in chemical kinetics. 3.) This method is based on the formation of covalent
5.) When the substrate concentration is low, the reaction bonds between the enzyme molecules by means of
rate is _____ with respect to the substrate. multifunctional reagents, leading to three dimensional cross
6.) At high substrate concentration the rate of reaction is linked aggregates. - cross linking
______. 4.) Biological catalysts that are protein in nature. - enzymes
7.) The movement of the enzyme in a fixed location is 5.) Original theory to account for the formation of the
restricted by attaching them to an insoluble support enzyme-substrate complex. – lock-and-key theory
medium or enclosed by the support medium which is also 6.) This procedure of immobilization is simple and it is
known as the carrier. possible to separate and purify the enzymes. - adsorption
8.) This method of enzyme immobilization has a major 7.) In this approach that the product releasing step is much
advantage in the fact that there is no chemical modification slower than the reversible reaction and the slow step
of the enzyme. determines the rate while the other is at equilibrium.
9.) This method is based on the formation of covalent 8.) When the substrate concentration is low, the reaction
bonds between the enzyme molecules by means of rate is _____ with respect to the substrate.
multifunctional reagents, leading to three dimensional cross 9.) At high substrate concentration the rate of reaction is
linked aggregates. ______.
10.) This procedure of immobilization is simple and it is 10.) This is also known as the pseudo-steady-state
possible to separate and purify the enzymes. assumption in chemical kinetics.

II. Problem Solving. II. Problem Solving.

1. A study was made to evaluate the constants so that the 1. Eadie (1942) measured the initial reaction rate of
Michaelis-Menten relationship could be used to describe hydrolysis of acetylcholme (substrate) by dog serum
waste utilization by bacteria. It was found that one gram of (source of enzyme) and obtained the following data:
bacteria could decompose the waste at a maximum rate of
20 grams per day when the waste concentration was high.
Also, it was found that this same quantity of bacteria would
decompose waste at a rate of 10 grams/day when the waste
concentration surrounding the bacteria was 15 mg/l. The
rate of waste decomposition by 2 grams of bacteria if the
waste concentration were maintained at 5 mg/l is______.

2. Eadie (1942) measured the initial reaction rate of


hydrolysis of acetylcholme (substrate) by dog serum
(source of enzyme) and obtained the following data:
Evaluate the Michaelis-Menten kinetic parameters by
employing (a) the Langmuir plot, (b) the Lineweaver-Burk
plot, (c) the Eadie-Hofstee plot

2. A study was made to evaluate the constants so that the


Michaelis-Menten relationship could be used to describe
waste utilization by bacteria. It was found that one gram of
bacteria could decompose the waste at a maximum rate of
20 grams per day when the waste concentration was high.
Also, it was found that this same quantity of bacteria would
Evaluate the Michaelis-Menten kinetic parameters by decompose waste at a rate of 10 grams/day when the waste
employing (a) the Langmuir plot, (b) the Lineweaver-Burk concentration surrounding the bacteria was 15 mg/l. The
plot, (c) the Eadie-Hofstee plot rate of waste decomposition by 2 grams of bacteria if the
waste concentration were maintained at 5 mg/l is______.
Quiz Set: ### Quiz Set: ####
Enzyme Kinetics and Immobilization Enzyme Kinetics and Immobilization
I. Identification I. Identification
Second order Lock-and-key theory Entrapment Second order Lock-and-key theory Entrapment
Third order Michaelis-Menten Briggs-Haldane Third order Michaelis-Menten Briggs-Haldane
Zero Order Cross Linking Adsorption Zero Order Cross Linking Adsorption
Enzymes Enzyme immobilization Enzymes Enzyme immobilization

1.) This procedure of immobilization is simple and it is 1.) This is also known as the pseudo-steady-state
possible to separate and purify the enzymes. assumption in chemical kinetics.
2.) This method is based on the formation of covalent 2.) At high substrate concentration the rate of reaction is
bonds between the enzyme molecules by means of ______.
multifunctional reagents, leading to three dimensional cross 3.) When the substrate concentration is low, the reaction
linked aggregates. rate is _____ with respect to the substrate.
3.) This method of enzyme immobilization has a major 4.) In this approach that the product releasing step is much
advantage in the fact that there is no chemical modification slower than the reversible reaction and the slow step
of the enzyme. determines the rate while the other is at equilibrium.
4.) The movement of the enzyme in a fixed location is 5.) This procedure of immobilization is simple and it is
restricted by attaching them to an insoluble support possible to separate and purify the enzymes.
medium or enclosed by the support medium which is also 6.) Original theory to account for the formation of the
known as the carrier. enzyme-substrate complex.
5.) At high substrate concentration the rate of reaction is 7.) Biological catalysts that are protein in nature.
______. 8.) This method is based on the formation of covalent
6.) When the substrate concentration is low, the reaction bonds between the enzyme molecules by means of
rate is _____ with respect to the substrate. multifunctional reagents, leading to three dimensional cross
7.) This is also known as the pseudo-steady-state linked aggregates.
assumption in chemical kinetics. 9.) This method of enzyme immobilization has a major
8.) In this approach that the product releasing step is much advantage in the fact that there is no chemical modification
slower than the reversible reaction and the slow step of the enzyme.
determines the rate while the other is at equilibrium. 10.) The movement of the enzyme in a fixed location is
9.) Original theory to account for the formation of the restricted by attaching them to an insoluble support
enzyme-substrate complex. medium or enclosed by the support medium which is also
10.) Biological catalysts that are protein in nature. known as the carrier.

II. Problem Solving. II. Problem Solving.

1. A study was made to evaluate the constants so that the 1. Eadie (1942) measured the initial reaction rate of
Michaelis-Menten relationship could be used to describe hydrolysis of acetylcholme (substrate) by dog serum
waste utilization by bacteria. It was found that one gram of (source of enzyme) and obtained the following data:
bacteria could decompose the waste at a maximum rate of
20 grams per day when the waste concentration was high.
Also, it was found that this same quantity of bacteria would
decompose waste at a rate of 10 grams/day when the waste
concentration surrounding the bacteria was 15 mg/l. The
rate of waste decomposition by 2 grams of bacteria if the
waste concentration were maintained at 5 mg/l is______.

2. Eadie (1942) measured the initial reaction rate of


hydrolysis of acetylcholme (substrate) by dog serum
(source of enzyme) and obtained the following data: Evaluate the Michaelis-Menten kinetic parameters by
employing (a) the Langmuir plot, (b) the Lineweaver-Burk
plot, (c) the Eadie-Hofstee plot

2. A study was made to evaluate the constants so that the


Michaelis-Menten relationship could be used to describe
waste utilization by bacteria. It was found that one gram of
bacteria could decompose the waste at a maximum rate of
20 grams per day when the waste concentration was high.
Also, it was found that this same quantity of bacteria would
decompose waste at a rate of 10 grams/day when the waste
Evaluate the Michaelis-Menten kinetic parameters by concentration surrounding the bacteria was 15 mg/l. The
employing (a) the Langmuir plot, (b) the Lineweaver-Burk rate of waste decomposition by 2 grams of bacteria if the
plot, (c) the Eadie-Hofstee plot waste concentration were maintained at 5 mg/l is______.