Dietary Proteins and Digestion
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Questions and Answers

Which of the following is a principal animal source of dietary protein?

  • Pulses
  • Liver (correct)
  • Nuts
  • Cereals

What is the main reason that proteins are not digested in the mouth?

  • Low pH levels
  • Inadequate saliva production
  • Absence of proteolytic enzymes (correct)
  • Insufficient chewing

Which enzyme acts on the N-terminal amino acids during protein digestion?

  • Aminopeptidase (correct)
  • Carboxypeptidase
  • Trypsin
  • Pepsin

What role does hydrochloric acid (HCl) play in protein digestion in the stomach?

<p>It activates pepsinogen to pepsin (A)</p> Signup and view all the answers

Which of the following enzymes is not produced in the stomach?

<p>Trypsin (A)</p> Signup and view all the answers

How is pepsinogen converted to pepsin?

<p>By hydrochloric acid (HCl) (C)</p> Signup and view all the answers

What is the typical range for daily intake of dietary protein?

<p>50-100 g/day (B)</p> Signup and view all the answers

Which of the following statements about peptide bonds is true?

<p>They link amino acids together (C)</p> Signup and view all the answers

What is the optimal pH range for the activity of pepsin?

<p>1.6 to 2.5 (C)</p> Signup and view all the answers

What is the role of rennin (chymosin) in digestion?

<p>Curdles milk by converting casein to calcium paracaseinate (D)</p> Signup and view all the answers

How is trypsin activated from its zymogen form?

<p>By other proteolytic enzymes in the duodenum (D)</p> Signup and view all the answers

Which of the following statements about pepsin is incorrect?

<p>Pepsin hydrolyzes peptide bonds selectively. (B)</p> Signup and view all the answers

What effect does cholecystokinin have on the digestive process?

<p>Stimulates the release of pancreatic juice (B)</p> Signup and view all the answers

What products result from the action of pepsin on proteins?

<p>Proteoses and peptones (A)</p> Signup and view all the answers

What is the molecular weight of pepsin?

<p>42,500 (C)</p> Signup and view all the answers

What is the primary function of gelatinase in gastric juice?

<p>To hydrolyze gelatin (C)</p> Signup and view all the answers

What is the primary function of enterokinase in the digestive process?

<p>To convert trypsinogen into trypsin (B)</p> Signup and view all the answers

Which of the following enzymes can only hydrolyze peptide bonds connected to proline residues?

<p>Prolidase (A)</p> Signup and view all the answers

Which factor is necessary for amino peptidases to effectively catalyze peptide hydrolysis?

<p>Presence of metal ions like Zn++, Mn++, and Mg++ (C)</p> Signup and view all the answers

Where does the absorption of released amino acids primarily occur in the digestive system?

<p>In the distal jejunum and ileum (D)</p> Signup and view all the answers

What distinguishes tri-peptidase from di-peptidase in their enzymatic activity?

<p>Di-peptidase hydrolyzes dipeptides to yield two amino acids. (D)</p> Signup and view all the answers

What characteristic defines the specificity of proteolytic enzymes during protein digestion?

<p>They exhibit specific cleavage patterns based on amino acid structure. (C)</p> Signup and view all the answers

What is a significant outcome of inadequate proteolytic enzyme activity during digestion?

<p>Presence of undigested oligopeptides in the intestine (B)</p> Signup and view all the answers

Which condition is necessary for the activation of trypsinogen into trypsin?

<p>Action of enterokinase (D)</p> Signup and view all the answers

Flashcards

Dietary protein sources

Dietary proteins are obtained from animal sources like milk, meat, and fish, and from vegetable sources like cereals, pulses, and beans.

Protein digestion

The process of breaking down proteins into smaller units through the action of enzymes.

Peptidases

Enzymes that break down proteins by cleaving the peptide bonds between amino acids.

Endopeptidases

Peptidases that act on the internal peptide bonds within a protein chain, releasing smaller peptide fragments.

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Exopeptidases

Peptidases that act on the terminal ends of a protein chain, removing single amino acids.

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Hydrochloric acid (HCL)

A strong acid produced in the stomach that helps break down food and kill harmful bacteria.

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Zymogen

An inactive form of an enzyme that needs to be activated to become functional. It's how pepsin is initially produced in the stomach.

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Pepsin

A powerful enzyme present in gastric juices that breaks down proteins into smaller peptides.

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Enterokinase (Enteropeptidase)

A glycoprotein enzyme that activates trypsinogen to trypsin, a key step in protein digestion.

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Aminopeptidases

Hydrolyze peptides into tripeptides, but cannot break down dipeptides. Requires Zn++, Mn++, Mg++ for activity.

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Prolidase

An exopeptidase that can break down the peptide bond between proline and another amino acid in collagen molecules.

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Tripeptidases and Dipeptidases

Break down tripeptides into dipeptides and amino acids. Dipeptidases further hydrolyze dipeptides into two amino acids.

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Protein Digestion in the Small Intestine

The breakdown of proteins into their constituent amino acids.

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Amino Acid Absorption

The process by which amino acids are absorbed into the body, primarily from the ileum and distal jejunum.

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Oligopeptides

Peptides, primarily tripeptides and dipeptides, that remain undigested after the primary protein digestion.

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Ileum and Distal Jejunum

The primary site of amino acid absorption, located in the lower part of the small intestine.

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Pepsinogen

The inactive form of pepsin, secreted in gastric juice and activated by HCl.

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Milk Curdling

The process of converting milk protein casein into calcium paracaseinate, making it easier to digest.

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Rennin (Chymosin)

An enzyme secreted in the stomach of infants, crucial for digesting milk.

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Gastriscin

An enzyme secreted as an inactive zymogen in gastric juice, activated by HCl and active at slightly less acidic pH than pepsin.

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Trypsinogen

A protein-digesting enzyme found in the pancreatic juice, secreted as an inactive zymogen.

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Trypsin

The active form of trypsinogen, a protein-digesting enzyme found in the small intestine.

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Duodenum

The first part of the small intestine where food mixes with pancreatic juice, containing enzymes for digestion.

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Study Notes

Dietary Proteins

  • Dietary proteins come from animal or vegetable sources
  • Principal animal sources include milk, dairy products, meat, fish, liver, and eggs.
  • Principal vegetable sources include cereals, pulses, peas, beans, and nuts.
  • Dietary protein intake is roughly 50-100 g/day.
  • Endogenous protein (digestive enzymes and worn-out cells) is about 28 g daily.
  • Protein loss through feces is minimal, approximately 5-10 g/day.

Digestion in the Mouth

  • No proteolytic enzymes are present in saliva.
  • Chewing breaks down food into smaller pieces ("bolus").
  • The bolus moves to the stomach to interact with gastric juice.

Protein Degradation

  • Proteins are broken down by hydrolases.
  • Hydrolases are enzymes classified as peptidases, cleaving peptide bonds.
  • Endopeptidases (proteases) attack internal peptide bonds, and produce fragments
  • Exopeptidases act on terminal amino acids

Digestion in the Stomach

  • Gastric juice contains proteolytic enzymes (e.g., pepsin, renin, gastricin).
  • Hydrochloric acid (HCl) is also present in gastric juice.
  • HCl lowers stomach pH to less than 2
  • HCl denatures proteins, making them more susceptible to proteases
  • Pepsin works optimally in highly acidic conditions (pH 1.6-2.5)
  • Pepsin is a proteinase that hydrolyses peptide bonds, forming smaller fragments
  • Rennin is present in infants and children; converting milk protein casein to paracaseinate, which pepsin digests more easily.
  • Gastricin is a protease active at a pH of 3 to 4.
  • Gelatinase hydrolyzes gelatin in an acidic medium

Digestion in the Duodenum

  • Food from the stomach enters the duodenum, where it mixes with pancreatic juice.
  • Pancreatic juice contains proteases that are secreted as proenzymes (zymogens).
  • Cholecystokinin and secretin stimulate release of pancreatic juice.
  • Pancreatic proteases include trypsin, chymotrypsin, carboxypeptidases, and elastases.
  • Trypsin, a proteinase, is secreted as trypsinogen (inactive form).
  • Enterokinase (enteropeptidase) activate trypsinogen to trypsin.
  • Trypsin is essential for activating other pancreatic proenzymes.

Digestion in the Small Intestine

  • Intestinal juice contains proteolytic enzymes (enterokinase, prolidase, aminopeptidases, dipeptidases, tripeptidases).
  • Enterokinase converts trypsinogen to trypsin.
  • Prolidase acts on proline containing peptides.
  • Aminopeptidases, dipeptidases, and tripeptidases help break down peptides into smaller fragments.

Absorption of Amino Acids

  • Amino acids are absorbed into the bloodstream from the small intestine's ileum and distal jejunum.
  • Some oligopeptides (dipeptides and tripeptides) are also absorbed, but then further broken down.
  • L-amino acids and L-peptides are absorbed faster than their D-isomers.
  • They typically enter the bloodstream passively via special transporters.

How amino acids reach the liver

  • Amino acids and digested products are absorbed from the intestines.
  • They are carried by the portal vein to the liver for further use in the body.

Overview of Protein Digestion

  • Food proteins enter the digestive tract.
  • Pepsin in the stomach breaks down proteins into smaller polypeptides.
  • In the small intestine, proteases and other enzymes continue breaking them down into amino acids.
  • Small fragments of peptides are also broken down into amino acids.
  • Amino acids are absorbed into the bloodstream and used by the body.

Enzyme Specificity

  • Enzymes have specificity, cleaving only certain peptide bonds.
  • Pepsin is active at low pHs, preferring peptide bonds with aromatic amino acids.
  • Trypsin prefers peptide bonds with Lys or Arg at the carboxyl terminal part of peptide bond.
  • Chymotrypsin works well on peptide bonds with aromatic amino acids on the carboxyl terminus.

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Description

This quiz covers the sources of dietary proteins, including both animal and vegetable origins, and discusses their daily intake. It also examines the process of digestion in the mouth and stomach, including the role of different enzymes in protein degradation. Test your knowledge on these essential topics!

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