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ICAR AICE-JRF/SRF Milk Proteins & Enzymes: practice questions

ICAR AICE-JRF/SRF (PhD): Dairy Chemistry, Dairy Microbiology, Dairy Technology, Dairy Engineering · India · NTA for ICAR

Original practice questions written to the published syllabus · not past papers
10worked here, free
86written to this exam in this subject
13syllabus units

What this subject covers

Caseins and the casein micelle, whey proteins, minor proteins, genetic variants, heat denaturation, and the indigenous milk enzymes used as process indicators.

In the exams: ICAR AICE subject 34 Unit 2; ICAR AIEEA-PG group 16; ASRB NET Dairy Chemistry

What ICAR AICE-JRF/SRF asks from it

ICAR AICE-JRF/SRF (PhD) — Dairy Chemistry (subject 34, Unit 2)

Structure and properties of the caseins and whey proteins, micelle models and stability, genetic polymorphism, heat-induced changes and protein interactions, and indigenous enzymes with their technological significance. Questions go to residue numbers, phosphorylation and cysteine content, the Phe105-Met106 bond, nanocluster and dual-binding models, HCT-pH profiles, plasmin and lipoprotein lipase behaviour, and the WPNI classification.

Where the 86 questions fall

How our questions for ICAR AICE-JRF/SRF spread across the units of Milk Proteins & Enzymes. Difficulty: 16 easy, 43 medium, 27 hard.

Heat denaturation of whey proteins and whey protein-casein interactions9
Caseins: alpha-s1, alpha-s2, beta and kappa8
Casein micelle structure and models7
Micelle stability: calcium phosphate, kappa-casein and zeta potential7
Genetic polymorphism of milk proteins, including A1 and A2 beta-casein7
Immunoglobulins, lactoferrin, lysozyme and lactoperoxidase7
Indigenous enzymes: alkaline phosphatase, lactoperoxidase, lipoprotein lipase, plasmin7
Classification of milk proteins and nitrogen fractions6
Whey proteins: beta-lactoglobulin and alpha-lactalbumin6
Enzyme indicators of heat treatment6
Bioactive peptides and protein hydrolysates6
Milk fat globule membrane proteins5
Milk protein allergenicity5

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 · Caseins: alpha-s1, alpha-s2, beta and kappa · easy

Which casein contains no cysteine and has five phosphate groups clustered near its N-terminus?

  1. Alpha-s2-casein
  2. Alpha-s1-casein
  3. Beta-casein
  4. Kappa-casein
Answer and working

C. Beta-casein

Beta-casein has 5 phosphoserines in its N-terminal region and no cysteine. Kappa- and alpha-s2-casein each have two cysteines; alpha-s1 has no cysteine but 8-9 phosphates.

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

2 · Caseins: alpha-s1, alpha-s2, beta and kappa · hard

Why are caseins described as rheomorphic or intrinsically disordered proteins?

  1. They fold into rigid beta-barrels that change shape only under shear
  2. They are cross-linked into a fixed tertiary structure by many disulphide bonds
  3. They are fully alpha-helical proteins that unfold reversibly at refrigeration temperatures and refold on warming
  4. They have a high proline content and few or no disulphide bonds, so they lack a stable folded structure
Answer and working

D. They have a high proline content and few or no disulphide bonds, so they lack a stable folded structure

Proline disrupts regular secondary structure and caseins have few disulphides, so they are open and flexible; this makes them heat-stable and easily hydrolysed. The beta-barrel describes beta-lactoglobulin.

Further reading: McSweeney and Fox (eds), Advanced Dairy Chemistry Vol. 1: Proteins

3 · Genetic polymorphism of milk proteins, including A1 and A2 beta-casein · hard

What did the 2009 scientific review commissioned by the European Food Safety Authority conclude about beta-casomorphins?

  1. A2 milk was proven to prevent heart disease and should replace A1 milk
  2. A1 beta-casein was proven to cause type 1 diabetes in children
  3. A cause-and-effect relationship with non-communicable diseases could not be established
  4. BCM-7 was shown to be absent from the digests of all beta-casein variants, including A1 and B
Answer and working

C. A cause-and-effect relationship with non-communicable diseases could not be established

The EFSA review found no established cause-effect link between BCM-7 and non-communicable diseases; the evidence is contested rather than settled.

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

4 · Genetic polymorphism of milk proteins, including A1 and A2 beta-casein · medium

In goats, the alpha-s1-casein gene has strong, weak and null alleles. What is their main technological effect?

  1. They change the amount of alpha-s1-casein secreted, with large effects on cheese yield and curd firmness
  2. They determine whether goat milk contains beta-lactoglobulin
  3. They change the colour of goat milk from white to yellow by altering carotene transport into the milk fat
  4. They control the size of fat globules and the rate of creaming
Answer and working

A. They change the amount of alpha-s1-casein secreted, with large effects on cheese yield and curd firmness

Goat alpha-s1-casein alleles differ greatly in expression; strong-allele milk has more casein, higher yield and firmer curd. Goat milk always contains beta-lactoglobulin.

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

5 · Genetic polymorphism of milk proteins, including A1 and A2 beta-casein · medium

Which milk is predominantly of the A2 beta-casein type?

  1. Milk from a herd of A1A1 Holstein cows
  2. Buffalo milk
  3. Milk from an A1A2 heterozygous herd
  4. Milk of any cow fed on pasture
Answer and working

B. Buffalo milk

Buffalo beta-casein has proline at the corresponding position, so it is A2-type. Diet does not change genotype.

Further reading: McSweeney and Fox (eds), Advanced Dairy Chemistry Vol. 1: Proteins

6 · Heat denaturation of whey proteins and whey protein-casein interactions · hard

Beta-lactoglobulin falls from 3.2 to 0.8 grams per litre of native protein after a heat treatment. What percentage was denatured?

  1. 80 per cent
  2. 40 per cent
  3. 25 per cent
  4. 75 per cent
Answer and working

D. 75 per cent

Denatured = (3.2 - 0.8)/3.2 x 100 = 75%. 25% is the share remaining native.

Further reading: McSweeney and Fox (eds), Advanced Dairy Chemistry Vol. 1: Proteins

7 · Enzyme indicators of heat treatment · medium

In the Aschaffenburg turbidity test, a filtrate that stays clear on boiling shows that the milk:

  1. Contained no remaining native whey protein, as in sterilised milk
  2. Contained added water or skim milk powder
  3. Was adequately pasteurised at minimum HTST conditions but not sterilised
  4. Was raw, with all whey proteins still native
Answer and working

A. Contained no remaining native whey protein, as in sterilised milk

After ammonium sulphate removes casein and denatured protein, any remaining native whey protein clouds the filtrate on boiling; clear filtrate indicates sterilisation.

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

8 · Bioactive peptides and protein hydrolysates · medium

If 0.9 milliequivalents of peptide bonds per gram are cleaved in casein (h-total 8.2 milliequivalents per gram), what is the degree of hydrolysis?

  1. 9.1 per cent
  2. 11.0 per cent
  3. 0.11 per cent
  4. 10.2 per cent
Answer and working

B. 11.0 per cent

DH = h/h-total x 100 = 0.9/8.2 x 100 = 11.0%. 10.2 uses the whey protein value 8.8; 0.11 forgets to multiply by 100.

Further reading: McSweeney and Fox (eds), Advanced Dairy Chemistry Vol. 1: Proteins

9 · Milk protein allergenicity · medium

Why do many children with milk allergy tolerate milk baked into foods but react to fresh milk?

  1. Baked foods contain no milk protein after cooking
  2. Heating destroys many conformational whey protein epitopes
  3. Baking removes lactose, the cause of allergic reactions
  4. Baking converts all casein epitopes into harmless amino acids
Answer and working

B. Heating destroys many conformational whey protein epitopes

Many whey epitopes are conformational and heat-labile; casein epitopes are mainly linear and survive heating, so baked milk is not tolerated by everyone.

Further reading: McSweeney and Fox (eds), Advanced Dairy Chemistry Vol. 1: Proteins

10 · Classification of milk proteins and nitrogen fractions · easy

A milk has 0.55 per cent total nitrogen. What is its crude protein using the milk factor?

  1. 8.62 per cent
  2. 3.44 per cent
  3. 3.51 per cent
  4. 0.09 per cent
Answer and working

C. 3.51 per cent

0.55 x 6.38 = 3.51%. 3.44 uses the general factor 6.25; 0.09 divides by 6.38.

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

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Milk Proteins & EnzymesThe full study manual, free ICAR AICE-JRF/SRFFormat, sections and how it has changed

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Milk Proteins & Enzymes for other exams

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