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GATE Biochemistry for Dairy Science: practice questions

GATE — Life Sciences (XL) with Section U Food Technology · India · IITs and IISc on rotation (2026: IIT Guwahati)

Original practice questions written to the published syllabus · not past papers
10worked here, free
69written to this exam in this subject
10syllabus units

What this subject covers

Carbohydrates, proteins, lipids, enzymes and metabolism at the level a dairy chemist and microbiologist needs before studying milk itself.

In the exams: Background for ICAR AICE subject 34 Units 1–3 and GATE XL-Q/XL-U Section 1

Where the 69 questions fall

How our questions for GATE spread across the units of Biochemistry for Dairy Science. Difficulty: 12 easy, 57 medium, 0 hard.

Carbohydrate structure and reactions8
Enzymes: classification and Michaelis-Menten kinetics8
Lipid and amino acid metabolism8
Nucleic acids and protein synthesis8
Vitamins as coenzymes and minerals8
Enzyme inhibition and regulation7
Glycolysis, TCA cycle and oxidative phosphorylation7
Amino acids, peptides and protein structure6
Water, pH and buffers5
Lipid classes and fatty acids4

10 practice questions, worked

Choose an answer, then open the working. Each explanation says why the right answer is right and why the others are not.

1 · Carbohydrate structure and reactions · medium

The interconversion of α- and β-anomers of lactose in solution until equilibrium is reached is called:

  1. Caramelisation
  2. Epimerisation by enzymes
  3. Mutarotation
  4. Saponification
Answer and working

C. Mutarotation

Through the open-chain form the anomers interconvert, changing optical rotation until equilibrium (about 37% α, 63% β for lactose at room temperature).

Further reading: Fox et al., Dairy Chemistry and Biochemistry

2 · Amino acids, peptides and protein structure · medium

Glycine has pKa values of 2.34 (carboxyl) and 9.60 (amino). What is its isoelectric point?

  1. 5.97
  2. 7.26
  3. 11.94
  4. 3.63
Answer and working

A. 5.97

pI = (2.34 + 9.60)/2 = 5.97. 11.94 is the sum without halving.

Further reading: Nelson and Cox, Lehninger Principles of Biochemistry

3 · Amino acids, peptides and protein structure · medium

An α-helix contains how many amino acid residues per turn?

  1. 3.6
  2. 2.0
  3. 10.5
  4. 4.5
Answer and working

A. 3.6

The right-handed α-helix has 3.6 residues per turn and a rise of 0.54 nm per turn. 10.5 is the number of base pairs per turn of B-DNA.

Further reading: Nelson and Cox, Lehninger Principles of Biochemistry

4 · Lipid classes and fatty acids · medium

Which pair are the essential fatty acids for humans?

  1. Palmitic (16:0) and stearic (18:0)
  2. Linoleic (18:2 n-6) and α-linolenic (18:3 n-3)
  3. Oleic (18:1 n-9) and butyric (4:0)
  4. Vaccenic (trans-11 18:1) and lauric (12:0)
Answer and working

B. Linoleic (18:2 n-6) and α-linolenic (18:3 n-3)

Humans cannot introduce double bonds beyond Δ9, so n-6 and n-3 parents must come from the diet.

Further reading: Nelson and Cox, Lehninger Principles of Biochemistry

5 · Enzyme inhibition and regulation · medium

β-Galactosidase hydrolysing lactose in milk slows down as the reaction proceeds partly because:

  1. Glucose irreversibly destroys the enzyme active site
  2. Lactose is an allosteric activator that is used up
  3. Galactose, a product, competitively inhibits the enzyme
  4. The pH of milk rises sharply as lactose is hydrolysed
Answer and working

C. Galactose, a product, competitively inhibits the enzyme

Galactose resembles the galactosyl part of lactose and competes for the active site of many β-galactosidases. Substrate depletion also reduces the rate.

Further reading: Fox et al., Dairy Chemistry and Biochemistry

6 · Glycolysis, TCA cycle and oxidative phosphorylation · medium

Why must lactic acid bacteria reduce pyruvate to lactate rather than simply accumulate pyruvate?

  1. To make extra ATP by substrate-level phosphorylation
  2. To produce CO₂ for gas holes
  3. To regenerate NAD⁺ so that glycolysis can continue
  4. To synthesise fatty acids for the membrane
Answer and working

C. To regenerate NAD⁺ so that glycolysis can continue

Glyceraldehyde 3-phosphate dehydrogenase needs NAD⁺; without respiration, reducing pyruvate is the way to reoxidise NADH. The LDH step itself makes no ATP.

Further reading: Nelson and Cox, Lehninger Principles of Biochemistry

7 · Nucleic acids and protein synthesis · medium

Antibiotics such as tetracyclines inhibit bacteria selectively because they act on:

  1. Bacterial 70S ribosomes, which differ from 80S ones
  2. DNA polymerase of all living cells equally, bacterial or animal
  3. The 80S ribosomes of the host
  4. Mitochondrial ATP synthase only
Answer and working

A. Bacterial 70S ribosomes, which differ from 80S ones

Structural differences between 70S and 80S ribosomes allow selective inhibition of bacterial protein synthesis.

Further reading: Nelson and Cox, Lehninger Principles of Biochemistry

8 · Vitamins as coenzymes and minerals · medium

The light-induced off-flavour of milk displayed under fluorescent lighting is initiated by which vitamin acting as a photosensitiser?

  1. Vitamin A
  2. Vitamin C
  3. Riboflavin
  4. Thiamine
Answer and working

C. Riboflavin

Riboflavin absorbs light and generates reactive species that oxidise methionine to methional and attack lipids; riboflavin itself is destroyed.

Further reading: Fox et al., Dairy Chemistry and Biochemistry

9 · Vitamins as coenzymes and minerals · medium

Biotin acts as the coenzyme of which type of reaction?

  1. Transamination
  2. Oxidative decarboxylation
  3. One-carbon transfer
  4. Carboxylation
Answer and working

D. Carboxylation

Biotin carries activated CO₂ in carboxylases such as acetyl-CoA carboxylase and pyruvate carboxylase.

Further reading: Nelson and Cox, Lehninger Principles of Biochemistry

10 · Vitamins as coenzymes and minerals · medium

Magnesium is required by virtually every enzyme that uses ATP because:

  1. Magnesium is part of the adenine ring
  2. Magnesium oxidises ATP to ADP
  3. The true substrate is the magnesium–ATP complex
  4. Magnesium is the coenzyme of all kinases in place of a vitamin
Answer and working

C. The true substrate is the magnesium–ATP complex

Mg²⁺ binds the phosphates of ATP, shielding charge and positioning it for catalysis.

Further reading: Nelson and Cox, Lehninger Principles of Biochemistry

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Read the subject

Biochemistry for Dairy ScienceThe full study manual, free GATEFormat, sections and how it has changed

More GATE practice

General MicrobiologyHuman Nutrition & Dairy in the DietDairy Analogues, Plant-based Alternatives & Composite Dairy FoodsFluid Flow, Thermodynamics & Heat Transfer in Dairy PlantsMathematics & Statistics for Dairy Science

Biochemistry for Dairy Science for other exams

ICAR AIEEA-PG · IndiaICAR AICE-JRF/SRF · India

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