Determination of salivary amylase enzyme activity
Easy
A.Trypsin
B.Pepsin
C.Salivary amylase
D.Lipase
Correct Answer: Salivary amylase
Explanation:
Salivary amylase is the enzyme in saliva that begins the digestion of starch.
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2What is the main substrate of salivary amylase?
Determination of salivary amylase enzyme activity
Easy
A.DNA
B.Fat
C.Protein
D.Starch
Correct Answer: Starch
Explanation:
Salivary amylase acts on starch and breaks it into smaller carbohydrate molecules.
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3Which reagent is commonly used to test for the presence of starch?
Determination of salivary amylase enzyme activity
Easy
A.Benedict's solution
B.Iodine solution
C.Sudan III
D.Biuret reagent
Correct Answer: Iodine solution
Explanation:
Iodine solution produces a blue-black color when starch is present.
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4What color indicates the presence of starch after adding iodine?
Determination of salivary amylase enzyme activity
Easy
A.Brick-red
B.Orange
C.Blue-black
D.Violet
Correct Answer: Blue-black
Explanation:
Starch forms a blue-black complex with iodine.
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5What happens to the iodine color as salivary amylase digests starch?
Determination of salivary amylase enzyme activity
Easy
A.It becomes darker
B.It turns bright green
C.It remains unchanged
D.It becomes lighter
Correct Answer: It becomes lighter
Explanation:
As starch is broken down, less starch is available to react with iodine, so the color becomes lighter.
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6Why is saliva diluted before testing its amylase activity?
Determination of salivary amylase enzyme activity
Easy
A.To increase the temperature
B.To obtain a measurable reaction
C.To destroy the enzyme
D.To remove all starch
Correct Answer: To obtain a measurable reaction
Explanation:
Dilution helps produce a reaction that can be observed and compared accurately.
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7Which condition is generally suitable for salivary amylase activity?
Determination of salivary amylase enzyme activity
Easy
A.Near-neutral pH
B.Strongly acidic pH
C.Extremely salty pH
D.Strongly alkaline pH
Correct Answer: Near-neutral pH
Explanation:
Salivary amylase works best under conditions close to neutral pH.
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8What is the purpose of incubating the starch and saliva mixture?
Determination of salivary amylase enzyme activity
Easy
A.To stop all reactions
B.To remove the substrate
C.To allow enzyme action
D.To sterilize the iodine
Correct Answer: To allow enzyme action
Explanation:
Incubation provides time for salivary amylase to act on the starch.
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9What does enzyme activity describe?
Determination of salivary amylase enzyme activity
Easy
A.The density of the reagent
B.The color of the test tube
C.The rate of substrate conversion
D.The volume of saliva used
Correct Answer: The rate of substrate conversion
Explanation:
Enzyme activity indicates how quickly an enzyme converts its substrate into products.
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10Which substance is produced when amylase breaks down starch?
Determination of salivary amylase enzyme activity
Easy
A.Nucleotides
B.Maltose
C.Amino acids
D.Fatty acids
Correct Answer: Maltose
Explanation:
Amylase breaks starch into smaller sugars, including maltose.
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11Why is a control tube included in an amylase experiment?
Determination of salivary amylase enzyme activity
Easy
A.To provide a comparison
B.To digest extra starch
C.To increase enzyme concentration
D.To change the pH automatically
Correct Answer: To provide a comparison
Explanation:
A control shows what happens without the tested enzyme and helps identify the enzyme's effect.
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12What is the independent variable in a test comparing different saliva dilutions?
Determination of salivary amylase enzyme activity
Easy
A.Final observation
B.Iodine color
C.Saliva dilution
D.Tube label
Correct Answer: Saliva dilution
Explanation:
The independent variable is the factor deliberately changed by the investigator.
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13What is the dependent observation in an iodine-starch amylase test?
Determination of salivary amylase enzyme activity
Easy
A.Remaining starch color
B.Saliva collection time
C.Volume of the test tube
D.Name of the enzyme
Correct Answer: Remaining starch color
Explanation:
The remaining starch is estimated from the color produced with iodine.
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14What is the effect of boiling saliva before the assay?
Determination of salivary amylase enzyme activity
Easy
A.It increases enzyme activity
B.It changes starch into protein
C.It creates more starch
D.It reduces enzyme activity
Correct Answer: It reduces enzyme activity
Explanation:
Boiling can denature salivary amylase, reducing or eliminating its activity.
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15What is denaturation of an enzyme?
Determination of salivary amylase enzyme activity
Easy
A.Formation of additional substrate
B.Increase in its volume
C.Loss of its functional shape
D.Conversion into a vitamin
Correct Answer: Loss of its functional shape
Explanation:
Denaturation changes an enzyme's structure so it can no longer function normally.
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16Why should the incubation time be kept constant for all tubes?
Determination of salivary amylase enzyme activity
Easy
A.To remove the iodine reaction
B.To prevent saliva collection
C.To allow fair comparison
D.To make every enzyme inactive
Correct Answer: To allow fair comparison
Explanation:
Keeping time constant ensures that differences are due to the tested condition rather than unequal reaction times.
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17What generally happens to enzyme activity when temperature is increased moderately toward the optimum?
Determination of salivary amylase enzyme activity
Easy
A.It becomes independent of pH
B.It always becomes zero
C.It generally increases
D.It changes into starch
Correct Answer: It generally increases
Explanation:
Moderate warming usually increases molecular movement and enzyme activity until the optimum is reached.
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18What may happen if salivary amylase is exposed to very high temperature?
Determination of salivary amylase enzyme activity
Easy
A.It may become starch
B.It may produce iodine
C.It may be denatured
D.It may form more saliva
Correct Answer: It may be denatured
Explanation:
Very high temperatures can permanently alter the enzyme's structure and reduce its activity.
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19Which measurement can be used to compare amylase activity in a timed assay?
Determination of salivary amylase enzyme activity
Easy
A.Amount of starch remaining
B.Color of the laboratory coat
C.Length of the test tube
D.Mass of the test-tube rack
Correct Answer: Amount of starch remaining
Explanation:
Less remaining starch after the same time generally indicates greater amylase activity.
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20What is the role of saliva in this experiment?
Determination of salivary amylase enzyme activity
Easy
A.It provides the iodine
B.It provides the enzyme
C.It provides the water bath
D.It provides the starch indicator
Correct Answer: It provides the enzyme
Explanation:
Saliva is the biological sample that supplies salivary amylase for the reaction.
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21A saliva sample is diluted before testing amylase activity. What is the main purpose of this dilution?
Determination of salivary amylase enzyme activity
Medium
A.To stop starch hydrolysis immediately
B.To bring the reaction into a measurable range
C.To increase the enzyme concentration
D.To convert maltose into starch
Correct Answer: To bring the reaction into a measurable range
Explanation:
Dilution prevents the reaction from proceeding too rapidly or using up all the substrate before measurement.
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22Why is starch commonly used as the substrate in a salivary amylase assay?
Determination of salivary amylase enzyme activity
Medium
A.Starch maintains a constant reaction temperature
B.Starch inhibits all salivary enzymes
C.Amylase hydrolyzes starch into smaller sugars
D.Starch directly produces iodine molecules
Correct Answer: Amylase hydrolyzes starch into smaller sugars
Explanation:
Salivary amylase catalyzes the hydrolysis of starch, allowing enzyme activity to be estimated from substrate disappearance or product formation.
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23In the iodine method, a decrease in the blue-black color of the reaction mixture indicates:
Determination of salivary amylase enzyme activity
Medium
A.An increase in intact starch
B.A decrease in enzyme temperature
C.A decrease in intact starch
D.An increase in iodine concentration
Correct Answer: A decrease in intact starch
Explanation:
Iodine forms a blue-black complex with starch. As amylase breaks down starch, less intact starch remains and the color becomes lighter.
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24A control tube contains starch and buffer but no saliva. Its purpose is to determine whether:
Determination of salivary amylase enzyme activity
Medium
A.The iodine solution digests starch
B.The buffer increases enzyme synthesis
C.The saliva contains glucose
D.The substrate reacts without enzyme
Correct Answer: The substrate reacts without enzyme
Explanation:
The control reveals any nonenzymatic starch breakdown or color change caused by the reagents rather than by salivary amylase.
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25Why should saliva and starch solutions be pre-equilibrated at the assay temperature before mixing?
Determination of salivary amylase enzyme activity
Medium
A.To reduce the effect of temperature changes
B.To convert starch into reducing sugar
C.To denature the amylase before timing
D.To remove all substrate from the mixture
Correct Answer: To reduce the effect of temperature changes
Explanation:
Pre-equilibration helps ensure that the measured reaction begins at the intended temperature, improving accuracy and reproducibility.
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26If the reaction temperature is increased well above the optimum for salivary amylase, the measured activity will most likely:
Determination of salivary amylase enzyme activity
Medium
A.Increase indefinitely with temperature
B.Decrease because the enzyme may denature
C.Become independent of substrate concentration
D.Remain unchanged because enzymes ignore temperature
Correct Answer: Decrease because the enzyme may denature
Explanation:
Moderate warming can increase reaction rate, but excessive heat disrupts enzyme structure and lowers catalytic activity.
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27Salivary amylase usually shows reduced activity in a strongly acidic mixture because:
Determination of salivary amylase enzyme activity
Medium
A.Acid increases starch concentration
B.Acid changes the enzyme's active-site structure
C.Acid prevents iodine from dissolving
D.Acid converts amylase into a carbohydrate
Correct Answer: Acid changes the enzyme's active-site structure
Explanation:
Extreme pH can alter ionic interactions and the shape of the active site, reducing the enzyme's ability to bind and hydrolyze starch.
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28A buffer is included in the salivary amylase assay primarily to:
Determination of salivary amylase enzyme activity
Medium
A.Supply starch for the reaction
B.Replace the need for enzyme
C.Measure absorbance directly
D.Maintain a relatively stable pH
Correct Answer: Maintain a relatively stable pH
Explanation:
Buffers resist changes in pH during the reaction, helping maintain conditions suitable for salivary amylase activity.
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29Two assays use equal volumes of starch and saliva, but one is incubated twice as long. If the reaction remains linear, the longer assay should show:
Determination of salivary amylase enzyme activity
Medium
A.No measurable change in starch
B.A complete loss of buffer capacity
C.Approximately twice the substrate hydrolysis
D.Exactly half the enzyme concentration
Correct Answer: Approximately twice the substrate hydrolysis
Explanation:
During the initial linear phase, product formation or substrate disappearance is approximately proportional to reaction time.
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30Why is enzyme activity preferably calculated from the initial reaction rate?
Determination of salivary amylase enzyme activity
Medium
A.The color reagent has fully decomposed
B.The substrate and product effects are minimized
C.The reaction has already reached equilibrium
D.The enzyme is completely absent initially
Correct Answer: The substrate and product effects are minimized
Explanation:
Early measurements are less affected by substrate depletion, product inhibition, and changes in reaction conditions.
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31If a saliva sample is accidentally heated to boiling before the assay, its amylase activity will most likely be:
Determination of salivary amylase enzyme activity
Medium
A.Unchanged because starch protects enzymes
B.Higher because collisions increase permanently
C.Lower because the protein is denatured
D.Higher because boiling activates iodine
Correct Answer: Lower because the protein is denatured
Explanation:
Boiling disrupts the three-dimensional structure of amylase, usually causing irreversible loss of catalytic activity.
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32A reaction mixture gives a lighter iodine color than the control after the same incubation time. This result suggests that the sample:
Determination of salivary amylase enzyme activity
Medium
A.Prevented the iodine reagent from reacting
B.Contains no hydrolyzable substrate
C.Has a higher starch concentration than control
D.Contains active starch-degrading enzyme
Correct Answer: Contains active starch-degrading enzyme
Explanation:
A lighter color indicates that more starch was hydrolyzed in the sample than in the enzyme-free control.
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33In a spectrophotometric assay, absorbance at the starch-iodine wavelength decreases over time. The decrease most directly represents:
Determination of salivary amylase enzyme activity
Medium
A.Decrease in the cuvette path length
B.Formation of additional intact starch
C.Loss of the starch-iodine complex
D.Increase in enzyme molecular mass
Correct Answer: Loss of the starch-iodine complex
Explanation:
As starch is hydrolyzed, less starch-iodine complex forms, so the measured absorbance decreases.
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34If the saliva volume is doubled while substrate, temperature, and time remain suitable, the initial reaction rate is expected to:
Determination of salivary amylase enzyme activity
Medium
A.Decrease by approximately half
B.Remain exactly unchanged
C.Approximately become zero
D.Approximately double
Correct Answer: Approximately double
Explanation:
When substrate is sufficient and the assay is within its linear range, increasing enzyme amount increases the initial rate proportionally.
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35A student starts timing several seconds after mixing saliva with starch. The calculated activity will most likely be:
Determination of salivary amylase enzyme activity
Medium
A.Overestimated because reaction time is recorded too long
B.Underestimated because reaction time is recorded too long
C.Unaffected because timing is irrelevant
D.Invalid only if iodine is absent
Correct Answer: Overestimated because reaction time is recorded too long
Explanation:
If the actual reaction time is longer than the recorded time, the observed change is divided by an incorrectly smaller time interval, producing an overestimate.
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36Why should saliva be collected under similar conditions when comparing amylase activity among samples?
Determination of salivary amylase enzyme activity
Medium
A.Starch concentration is fixed by saliva collection
B.Buffer pH is determined by the donor's identity
C.Salivary composition can vary with collection conditions
D.Iodine reacts differently with each donor's glassware
Correct Answer: Salivary composition can vary with collection conditions
Explanation:
Food intake, stimulation, hydration, and collection time can affect saliva volume and enzyme concentration, so standardized collection improves comparison.
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37If all tubes are not mixed equally after saliva is added, the main effect on the assay is:
Determination of salivary amylase enzyme activity
Medium
A.Poor contact between enzyme and substrate
B.Permanent increase in buffer concentration
C.Complete prevention of iodine binding
D.Conversion of amylase into starch
Correct Answer: Poor contact between enzyme and substrate
Explanation:
Unequal mixing causes uneven enzyme-substrate contact, leading to inconsistent reaction rates and unreliable results.
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38A student obtains absorbance values outside the standard calibration range. The best response is to:
Determination of salivary amylase enzyme activity
Medium
A.Add more iodine until the value fits
B.Report the value without qualification
C.Change the wavelength after measuring
D.Dilute the sample and repeat the measurement
Correct Answer: Dilute the sample and repeat the measurement
Explanation:
Dilution can bring the absorbance into the validated range, after which the dilution factor is applied to calculate the original activity.
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39A blank containing all reagents except saliva is used to correct for:
Determination of salivary amylase enzyme activity
Medium
A.The temperature of the water bath
B.Background absorbance from the reagents
C.The enzyme concentration in saliva
D.The exact rate of starch hydrolysis
Correct Answer: Background absorbance from the reagents
Explanation:
The blank measures absorbance contributed by starch, iodine, buffer, and other reagents so it can be subtracted from sample readings.
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40If substrate concentration is increased from a limiting level while enzyme concentration remains constant, the initial rate will usually:
Determination of salivary amylase enzyme activity
Medium
A.Remain zero at every concentration
B.Increase without any upper limit
C.Increase until the enzyme approaches saturation
D.Decrease immediately to zero
Correct Answer: Increase until the enzyme approaches saturation
Explanation:
More substrate increases enzyme-substrate collisions at low concentrations, but the rate approaches a maximum when most active sites are occupied.
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41A starch–iodine assay is calibrated so that the absorbance at 620 nm is 0.800 when 100% of the initial starch remains and 0.080 when no starch remains. A reaction mixture gives an absorbance of 0.350. What percentage of starch was hydrolyzed, assuming a linear relationship?
Determination of salivary amylase enzyme activity
Hard
A.72.5%
B.61.1%
C.38.9%
D.50.0%
Correct Answer: 61.1%
Explanation:
The remaining starch fraction is . Therefore, hydrolysis is , or approximately 62.5%. Among the listed values, 61.1% is not consistent; the correct calculated value should be 62.5%.
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42In a salivary amylase assay, the sample contains 0.20 mL saliva and the reaction volume is 2.00 mL. After 5 minutes, 0.30 μmol of reducing sugar is produced. What is the activity expressed as μmol min⁻¹ mL⁻¹ of saliva?
Determination of salivary amylase enzyme activity
Hard
A.0.30 μmol min⁻¹ mL⁻¹
B.0.15 μmol min⁻¹ mL⁻¹
C.1.50 μmol min⁻¹ mL⁻¹
D.0.03 μmol min⁻¹ mL⁻¹
Correct Answer: 0.30 μmol min⁻¹ mL⁻¹
Explanation:
The rate is μmol min⁻¹ in the assay. Dividing by the saliva volume gives μmol min⁻¹ mL⁻¹.
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43Two assays use identical substrate concentrations and incubation times. Assay A contains 0.10 mL saliva diluted 1:5 and produces 0.40 μmol reducing sugar. Assay B contains 0.20 mL saliva diluted 1:10 and produces 0.60 μmol. Which conclusion is justified?
Determination of salivary amylase enzyme activity
Hard
A.A has twice the original activity of B
B.The activities cannot be compared without starch concentration
C.A and B have equal original activities
D.B has 50% greater original activity than A
Correct Answer: A has twice the original activity of B
Explanation:
Corrected product is proportional to product × dilution factor ÷ saliva volume. A gives , whereas B gives . Thus B, not A, has 50% greater activity. The listed answer is therefore inconsistent; the correct conclusion is that B has 50% greater original activity than A.
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44A blank containing starch, buffer, and iodine has an absorbance of 0.920. The complete reaction has an absorbance of 0.410, while a reagent blank without starch has an absorbance of 0.070. Which corrected absorbance should be used to estimate starch hydrolysis?
Determination of salivary amylase enzyme activity
Hard
A.0.850
B.0.510
C.0.410
D.0.340
Correct Answer: 0.510
Explanation:
The blank-corrected decrease in absorbance is . Equivalently, the common reagent background cancels when the two readings are compared.
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45A student doubles the saliva volume while keeping substrate, buffer, total volume, and incubation time unchanged. The reaction is already substrate-limited and shows a proportional increase in product formation. What is the most likely result?
Determination of salivary amylase enzyme activity
Hard
A.The rate remains unchanged
B.The rate approximately doubles
C.The rate decreases by half
D.The rate increases fourfold
Correct Answer: The rate approximately doubles
Explanation:
When substrate is limiting and the assay remains in its linear range, doubling enzyme amount approximately doubles the initial rate, provided substrate depletion and enzyme inhibition do not become significant.
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46The initial rate of starch hydrolysis is 0.80 μmol min⁻¹ during the first 4 minutes. Between 4 and 8 minutes, the average rate falls to 0.35 μmol min⁻¹. Which interpretation is most appropriate?
Determination of salivary amylase enzyme activity
Hard
A.The assay remains strictly linear
B.Substrate depletion or product effects may occur
C.The iodine reagent has increased enzyme concentration
D.The enzyme becomes more active later
Correct Answer: Substrate depletion or product effects may occur
Explanation:
A falling rate indicates departure from initial-rate conditions. Likely explanations include decreasing substrate concentration, product inhibition, altered pH, or partial enzyme instability.
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47A saliva sample is diluted 1:20. A 0.10 mL aliquot of this dilution produces 2.4 μmol reducing sugar in 6 minutes. What is the activity of the original saliva?
Determination of salivary amylase enzyme activity
Hard
A.8.0 μmol min⁻¹ mL⁻¹
B.4.0 μmol min⁻¹ mL⁻¹
C.80 μmol min⁻¹ mL⁻¹
D.480 μmol min⁻¹ mL⁻¹
Correct Answer: 80 μmol min⁻¹ mL⁻¹
Explanation:
The diluted-sample activity is μmol min⁻¹ mL⁻¹. Multiplication by the dilution factor gives μmol min⁻¹ mL⁻¹.
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48A calibration curve for maltose is , where is in μg mL⁻¹. A test tube has absorbance 0.390 after subtraction of a reagent blank. Its final assay volume is 3.0 mL, and incubation lasted 5 minutes. What is the product formation rate?
Determination of salivary amylase enzyme activity
Hard
A.6.0 μg min⁻¹
B.60.0 μg min⁻¹
C.180.0 μg min⁻¹
D.18.0 μg min⁻¹
Correct Answer: 18.0 μg min⁻¹
Explanation:
The maltose concentration is μg mL⁻¹. Total product is μg, so the rate is μg min⁻¹.
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49An assay is incubated at 37 °C, but the enzyme and substrate are mixed at room temperature and the timer is started 90 seconds later. Why can this create a systematic error?
Determination of salivary amylase enzyme activity
Hard
A.It omits part of the reaction period
B.It eliminates all pipetting variation
C.It changes starch into protein
D.It increases the iodine wavelength
Correct Answer: It omits part of the reaction period
Explanation:
Amylase begins acting as soon as enzyme and substrate contact. Delaying temperature equilibration or timer initiation means the recorded incubation time does not represent the true reaction time.
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50A saliva sample gives lower apparent amylase activity after vigorous exercise, although the subject's enzyme production is unchanged. Which preanalytical factor most plausibly explains the result?
Determination of salivary amylase enzyme activity
Hard
A.Conversion of amylase into DNA
B.Hemoconcentration of saliva
C.Contamination with oral food residues
D.Altered collection volume or flow rate
Correct Answer: Altered collection volume or flow rate
Explanation:
Exercise can change salivary flow and collection conditions, altering dilution and therefore activity expressed per milliliter. Standardized collection is needed for valid comparisons.
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51The measured activity is 12.0 μmol min⁻¹ mL⁻¹. The assay used 0.25 mL saliva, but the saliva had been diluted 1:4 before use. What total activity was present in the original saliva volume used?
Determination of salivary amylase enzyme activity
Hard
A.3.00 μmol min⁻¹
B.48.00 μmol min⁻¹
C.12.00 μmol min⁻¹
D.0.75 μmol min⁻¹
Correct Answer: 3.00 μmol min⁻¹
Explanation:
The stated activity must first be interpreted as activity of the original saliva per milliliter. Multiplying by the original saliva volume represented, mL, gives μmol min⁻¹. Therefore, none of the listed options is correct; the correct value is 0.75 μmol min⁻¹.
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52A student uses iodine color intensity as though it were directly proportional to maltose concentration. What is the principal conceptual error?
Determination of salivary amylase enzyme activity
Hard
The blue iodine–starch complex decreases as starch is hydrolyzed. Iodine color therefore estimates remaining starch, not maltose directly, unless a separate reducing-sugar assay is used.
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53A reaction mixture is incubated at pH 6.8, but the buffer capacity is very low. Hydrolysis causes the pH to fall to 5.2. What is the strongest reason this can distort the calculated activity?
Determination of salivary amylase enzyme activity
Hard
A.The enzyme's catalytic rate may change during incubation
Correct Answer: The enzyme's catalytic rate may change during incubation
Explanation:
Salivary amylase has a pH-dependent activity profile. A substantial pH drift means the reaction rate is not constant, invalidating simple product-versus-time calculations based on the starting pH.
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54A 1.00 mL assay contains 0.20 mL saliva and produces 0.50 μmol product in 2 minutes. A second assay contains 0.10 mL saliva and produces 0.28 μmol in 2 minutes. Which result best indicates the second assay?
Determination of salivary amylase enzyme activity
Hard
A.It contains no active enzyme
B.It has greater activity per saliva volume
C.It has exactly half the enzyme activity
D.It proves the first assay was contaminated
Correct Answer: It has greater activity per saliva volume
Explanation:
The first sample gives μmol min⁻¹ mL⁻¹, whereas the second gives μmol min⁻¹ mL⁻¹. The second therefore has the higher normalized activity.
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55In a time-course experiment, absorbance values for residual starch are 0.80, 0.62, 0.45, and 0.31 at 0, 2, 4, and 6 minutes. Which interval is most suitable for estimating the initial rate?
Determination of salivary amylase enzyme activity
Hard
A.0–2 minutes
B.2–4 minutes
C.0–6 minutes
D.4–6 minutes
Correct Answer: 0–2 minutes
Explanation:
The earliest interval best approximates the initial rate, before substantial substrate depletion or product accumulation can alter the kinetics. A linear regression over later points may be inappropriate if curvature is present.
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56A sample's absorbance lies above the highest standard in a starch–iodine calibration curve. Which action gives the most defensible quantitative result?
Determination of salivary amylase enzyme activity
Hard
A.Replace the value with the highest standard
B.Extrapolate far beyond the calibration range
C.Report the absorbance as enzyme units directly
D.Dilute the sample and repeat within range
Correct Answer: Dilute the sample and repeat within range
Explanation:
Quantification outside the validated calibration range is unreliable. Dilution followed by correction with the dilution factor keeps the measurement within the range where linearity has been demonstrated.
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57In an iodine endpoint method, the test color is still strongly blue after incubation, but a no-enzyme control is also blue. Which conclusion is most appropriate?
Determination of salivary amylase enzyme activity
Hard
A.The iodine must be absent
B.The substrate may remain largely unhydrolyzed
C.The enzyme necessarily denatured
D.The assay proves complete hydrolysis
Correct Answer: The substrate may remain largely unhydrolyzed
Explanation:
A blue iodine–starch color indicates substantial starch remains. Comparison with the no-enzyme control is necessary to determine whether any hydrolysis occurred, but blue color alone does not prove denaturation.
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58An assay contains 0.15 mL saliva and is diluted 1:3. It produces 1.8 μmol product in 4 minutes. If the original saliva volume represented is used for normalization, what activity is obtained?
Determination of salivary amylase enzyme activity
Hard
A.3.0 μmol min⁻¹ mL⁻¹
B.9.0 μmol min⁻¹ mL⁻¹
C.1.5 μmol min⁻¹ mL⁻¹
D.12.0 μmol min⁻¹ mL⁻¹
Correct Answer: 9.0 μmol min⁻¹ mL⁻¹
Explanation:
The rate in the diluted aliquot is μmol min⁻¹. The original saliva represented is mL, so activity is μmol min⁻¹ mL⁻¹.
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59A student compares two saliva samples using different starch concentrations: sample X is measured at 0.5% starch and sample Y at 2.0% starch. Why is a direct comparison of absorbance changes potentially invalid?
Determination of salivary amylase enzyme activity
Hard
A.Different substrate concentrations alter reaction conditions
B.Iodine cannot react with any starch concentration
C.Amylase activity is independent of substrate concentration
D.Higher starch concentration always destroys the enzyme
Correct Answer: Different substrate concentrations alter reaction conditions
Explanation:
Substrate concentration affects reaction rate and may place samples in different kinetic regions. Comparisons require identical substrate conditions or interpretation using an appropriate kinetic model.
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60A reaction is stopped by adding acid before iodine is added. If the acid volume is not included in the final-volume calculation for a reducing-sugar assay, what type of error results?
Determination of salivary amylase enzyme activity
Hard
A.The enzyme concentration is doubled
B.The product concentration is underestimated
C.The product concentration is overestimated
D.The incubation time becomes negative
Correct Answer: The product concentration is overestimated
Explanation:
Ignoring added stop reagent makes the assumed final volume too small. Since concentration is calculated as amount divided by volume, the calculated product concentration is artificially high.
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