Enzyme Activity Factors Quiz

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Questions and Answers

What is the relationship between enzyme concentration and reaction rate?

  • Enzyme concentration does not affect reaction rate
  • Reaction rate is directly proportional to enzyme concentration (correct)
  • Decreased enzyme concentration increases reaction rate
  • Increased enzyme concentration decreases reaction rate

At what temperature is the enzymatic activity maximally active?

  • 37-45°C (correct)
  • 70°C
  • 100°C
  • 0°C

What happens to enzymes at extremely high temperatures?

  • They are denatured and inactive (correct)
  • They become more active
  • They convert to co-enzymes
  • They increase substrate concentration

How does pH affect enzyme activity?

<p>Extreme pH levels can denature enzymes (A)</p>
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What is the effect of temperature increase on enzyme activity?

<p>Activity doubles for every 10°C increase until optimum temperature (A)</p>
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What term describes the temperature at which enzyme activity is maximized?

<p>Optimum temperature (C)</p>
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Which of the following is NOT a factor affecting enzyme activity?

<p>Colloid concentration (B)</p>
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What role does renin enzyme play in relation to milk protein?

<p>It helps in the clotting of milk protein (B)</p>
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What is the primary function of the rennin enzyme in milk digestion?

<p>To clot milk protein for digestion (C)</p>
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At what pH does rennin enzyme act optimally?

<p>pH 6 (A)</p>
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Why does rennin not act effectively in adults?

<p>Stomach acidity is too low for rennin activity (A)</p>
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What is produced after the enzymatic reaction of rennin on caseinogen?

<p>Casein (soluble) and small polypeptide (A)</p>
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Which component is essential for the formation of calcium caseinate?

<p>Calcium ions (Ca++) (B)</p>
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Which step in milk clotting involves the reaction between casein and calcium?

<p>Chemical reaction (C)</p>
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What is a key characteristic of whey after milk clotting?

<p>Greenish yellow due to vitamin B2 content (C)</p>
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What are the characteristics of rennin in relation to its type of enzyme?

<p>It is a hydrolase enzyme. (A)</p>
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Which temperature resulted in the fastest clotting time for rennin activity?

<p>37°C water bath (A)</p>
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What was observed in Tube No.3 after boiling the rennin enzyme?

<p>No clotting occurred (C)</p>
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How does the concentration of rennin affect its activity?

<p>Higher concentration results in faster clotting (B)</p>
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What effect did ammonium oxalate have on clotting in the prepared tubes?

<p>Completely precipitated calcium (D)</p>
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After boiling one of the test tubes and adding CaCl2, what was the result?

<p>Clotting occurred immediately (C)</p>
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Which of the following factors was stated not to be a co-enzyme for rennin?

<p>Calcium (D)</p>
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What role do enzymes play in chemical reactions?

<p>They catalyze the reactions without being altered (D)</p>
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What happens when the temperature is set too high for rennin activity?

<p>Enzyme may become denatured (B)</p>
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Study Notes

Enzymes

  • Catalyze biological reactions
  • Are proteins
  • Synthesized by cells

Factors Affecting Enzyme Activity

  • Substrate Concentration: Increased substrate concentration increases reaction rate until saturation point.
  • Enzyme Concentration: Increased enzyme concentration directly increases reaction rate.
  • Co-enzyme Concentration: Coenzymes are often required for enzyme function.
  • Product Concentration: Increased product concentration can inhibit enzyme activity.
  • Temperature:
    • Enzymes are inactive at 0°C.
    • Activity increases with temperature up to the optimum temperature (often 37-45°C).
    • Further temperature increase decreases activity due to denaturation.
    • Enzymes have different optimum temperatures.
  • pH:
    • Enzymes have an optimal pH for maximum activity.
    • Activity decreases above or below this pH.
    • Extreme pH values can denature enzymes.
  • Activators and Inhibitors:
    • Activators increase enzyme activity.
    • Inhibitors decrease enzyme activity.
  • Time: Prolonged exposure can affect enzyme activity.

Renin Enzyme

  • Found in the stomach of young calves and infants.
  • Digests caseinogen into casein.
  • Hydrolyzes caseinogen, splitting a polypeptide chain.
  • Optimum pH is 6, and temperature is 37°C.
  • Inactive in adults due to low stomach acidity (pH 1.5-2).

Milk Composition

  • Contains macronutrients (proteins, fats, carbohydrates), minerals (especially calcium and phosphorus), but low in copper and iron

Milk Proteins

  • High biological value
  • Caseinogen (60%):
    • A phosphoprotein
    • Digested by renin
  • Lactalbumin and Lactglobulin (40%): Simple soluble proteins

Milk Clotting

  • Renin clots milk, separating it into a solid clot and a liquid whey.
  • Promotes milk retention in the stomach for proper protein digestion.
  • Two-step process:
    1. Enzymatic Reaction: Renin hydrolyzes caseinogen into casein (soluble) and a small polypeptide.
    2. Chemical Reaction: Calcium ions react with casein, forming calcium caseinate (insoluble).

Calcium Caseinate

  • Precipitates, entangling with:
    • Milk fat
    • Fat-soluble vitamins
    • Carotenes
  • Forms the milk clot

Whey

  • Liquid phase, containing:
    • Water
    • Water-soluble vitamins
    • Lactalbumin
    • Lactglobulin
    • Lactose
    • Minerals (except calcium)
  • Greenish-yellow color due to vitamin B2 content.

Experimental Evidence

Effect of Temperature on Rennin Activity

  • Milk clots faster at 37°C than at room temperature (optimal temperature).
  • Boiled renin is inactive (denatured).

Effect of Concentration on Rennin Activity

  • Higher renin concentration leads to faster clotting.

Role of Calcium on Milk Clotting

  • Ammonium oxalate precipitates calcium, preventing clotting.
  • Adding calcium chloride to boiled, calcium-free milk results in clotting.
  • Calcium is essential for the precipitation of casein, not as a co-enzyme for renin.

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