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Enzyma'c

ac'vity of
Salivary Amylase: Eect of
pH and Temperature

Dharmatov Rahula B. Albano, Ph.D.
Department of Chemistry, College of Science


Enzymes
Large protein molecules specialized to catalyze
biological reactions (lowers activation energy)
Very specific and have extraordinary catalytic
power (acts on a specific substrate)
Reusable and remain unchanged
Operate at very high speed
Works in a two-step reaction process
E + S ES
ES E + P
The specificity of the enzyme is affected by pH,
temperature, and substrate concentration
Enzyme Classification
Naming Enzymes
Trivial (e.g. Trypsin and pepsin)
Substrate + ase ending (e.g. Sucrase)
Action + ase ending (e.g. Dehydrogenase)
Combo + ase ending (e.g. succinic acid
dehydrogenase, substrate = succinic acid,
action = removes H+, enzyme = ase ending)
Numerical (used more often in chemistry)
Salivary amylase EC 3.2.1.1
Influence of pH
Starch act as the substrate
Amylase enzyme
NaCl to mimic the normal physiological
condition in the body (amylase needs Cl to be
able to perform its function
pH Buffer variable
Condition (37 oC, constant) normal body
temperature
Influence of pH
Salivary amylase digestive enzyme
responsible for catalyzing the reaction:
Influence of pH

Starch occurs in two forms, -amylose and


amylopectin
-Amylose linear with -(1 4) glycosidic
linkages
Amylopectin contains two glycosidic
linkages, -(1 4) (linear) and -(1 6)
(branched)
Major components of starch can enzymatically
hydrolyzed by -amylase
Influence of pH

Amylodextrin, Erythrodextrin, Achrodextrin


smaller polysaccharides initially formed

Addition of Iodine (I2)


Blue solution (presence of starch)
Yellow solution (complete hydrolysis
disappearance of starch
Influence of pH
pH affects the conformation of the enzyme
Acidic/basic medium the enzyme is
denatured change in conformation 3o
structure
pH denaturation
Influence of pH
Optimum pH activity of the enzyme is at its
maximum hydrolyzes the starch at the least
time
At lower pH, the activity of the enzyme
increases until it reach the optimum
After the optimum pH, the enzyme activity
decreases
Optimum pH = 6.7; the pH of saliva of a
normal healthy individual is 6.5
Influence of Temperature
Starch act as the substrate
Amylase enzyme
NaCl to mimic the normal physiological
condition in the body (amylase needs Cl to be
able to perform its function
Temperature variable
Buffer pH 6.7 (constant) normal body
condition
Influence of Temperature

At LOW Temp, amylase is ineffective because


it is inactive
At HIGH Temp, the amylase becomes less
effective due to thermal denaturation
(amylase becomes permanently denatured)
Optimum temp = 37 deg C (maximum
amount of product is formed)
Rate of reaction = 1/time
Influence of the Substrate
Keeping the concentration of the enzyme constant while
increasing the concentration of substrate results in an
increase in the rate of reaction
At a certain concentration, the rate of reaction reaches a
maximum level (After increasing the substrate level does
not increase the rate of reaction)
Which bond is hydrolyzed by the salivary amylase?

In your mouth, where the pH is about 7, salivary amylase begins the digestion of starch.
When you swallow the saliva-food mixture and it reaches your stomach (pH 2), salivary
amylase stops catalyzing the breakdown of starch. Why?

What will happen if the carbohydrate taken by an individual is not fully hydrolyzed
(metabolized) in the body?

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