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Question

Identify the function of the enzyme trypsin.

This question was previously asked in
SSC CGL 2022 Tier-II (Paper 2 JSO) Previous Year Paper (04-Mar-2023)
The correct answer is

Digesting proteins

Understanding Enzyme Functions in Digestion

The question asks about the specific function of the enzyme trypsin within the digestive system. Enzymes are biological catalysts that speed up chemical reactions in the body. In digestion, enzymes break down large food molecules into smaller ones that can be absorbed.

What is Trypsin?

Trypsin is a powerful digestive enzyme. It is produced in an inactive form called trypsinogen by the pancreas. Trypsinogen is then activated into trypsin in the small intestine, primarily by another enzyme called enterokinase. Trypsin itself can also activate more trypsinogen, creating a chain reaction.

Trypsin's Primary Role: Protein Digestion

The main function of active trypsin in the small intestine is to break down proteins. Proteins are long chains of amino acids linked by peptide bonds. Trypsin is a type of protease, also known as a peptidase, which specifically targets and breaks these peptide bonds through a process called hydrolysis.

Trypsin acts on partially digested proteins (polypeptides) coming from the stomach and breaks them down into smaller polypeptides and peptides. Other enzymes, like chymotrypsin and carboxypeptidase (also from the pancreas), work alongside trypsin to further break down these protein fragments into even smaller peptides and individual amino acids, which can then be absorbed.

So, the core function of trypsin is centered around the digestion of proteins.

Analyzing the Options for Trypsin Function

Let's look at the provided options and determine which one accurately describes the function of trypsin:

  • Digesting proteins: As discussed, trypsin is a key enzyme responsible for breaking down proteins into smaller peptides. This aligns with its known biological role.
  • Breaking down carbohydrates: Carbohydrate digestion is primarily carried out by enzymes like amylase (in saliva and pancreatic juice). Trypsin does not digest carbohydrates.
  • Digesting roughage and fats: Roughage, mainly cellulose (a type of carbohydrate), is not digested by human enzymes; it acts as fiber. Fat digestion is primarily done by lipase enzymes, often with the help of bile for emulsification. Trypsin has no role in digesting roughage or fats.
  • Emulsifying insulin: Insulin is a hormone, not a food molecule to be digested in this manner. Furthermore, emulsification is a physical process (breaking large fat droplets into smaller ones) performed by bile salts, not enzymes like trypsin, and it applies to fats, not proteins or hormones like insulin.

Conclusion: Identifying Trypsin's Role

Based on the functions of digestive enzymes, trypsin is specifically involved in the breakdown of proteins. It hydrolyzes peptide bonds within protein chains, breaking them into smaller segments.

Enzyme Source Primary Function Target Molecule
Amylase Salivary glands, Pancreas Breaks down carbohydrates (starch) Carbohydrates
Lipase Pancreas, Stomach, Salivary glands Breaks down fats (triglycerides) Fats
Trypsin Pancreas (as trypsinogen) Breaks down proteins (polypeptides) Proteins
Chymotrypsin Pancreas (as chymotrypsinogen) Breaks down proteins (polypeptides) Proteins
Carboxypeptidase Pancreas (as procarboxypeptidase) Breaks down proteins (peptides) Proteins

Therefore, the function of the enzyme trypsin is digesting proteins.

Revision Table: Key Digestive Enzymes

Enzyme Name Function
Trypsin Protein digestion (breaks peptide bonds)
Amylase Carbohydrate digestion (starch breakdown)
Lipase Fat digestion (triglyceride breakdown)
Pepsin Protein digestion (in stomach)
Lactase Lactose digestion

Additional Information: Protein Digestion Process

Protein digestion begins in the stomach with the enzyme pepsin, which breaks down large proteins into smaller polypeptides in the acidic environment. When these polypeptides move into the small intestine, the environment becomes alkaline. Here, pancreatic proteases like trypsin, chymotrypsin, and carboxypeptidase become active. Trypsin and chymotrypsin break polypeptides into smaller peptide chains, while carboxypeptidase cleaves off amino acids from the carboxyl end of peptides. Further breakdown into individual amino acids and very small peptides occurs through enzymes on the brush border of the small intestine lining (like aminopeptidases and dipeptidases). Only amino acids and di/tripeptides are absorbed into the bloodstream.

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