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ICAR AICE-JRF/SRF Advanced Dairy Chemistry: 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
99written to this exam in this subject
10syllabus units

What this subject covers

Graduate-level protein, lipid and lactose chemistry, reaction kinetics and the physical chemistry of processing, as examined in ICAR AICE subject 34.

In the exams: ICAR AICE subject 34 (all units); ASRB NET Dairy Chemistry

Where the 99 questions fall

How our questions for ICAR AICE-JRF/SRF spread across the units of Advanced Dairy Chemistry. Difficulty: 2 easy, 73 medium, 24 hard.

Chemical and enzyme kinetics in milk systems10
Protein-protein interactions under heat and pressure10
Structure-function of casein micelles under processing10
Lipid oxidation chemistry and flavour10
Maillard reaction pathways and advanced glycation products10
Mineral equilibria modelling10
Proteomics, lipidomics and metabolomics of milk10
Authenticity and origin testing10
Bioactive components and their analysis10
Water activity, glass transition and state diagrams9

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 · Chemical and enzyme kinetics in milk systems · hard

Using z ≈ 2.303RT²/Eₐ, estimate z at 120 °C (393 K) for a browning reaction with Eₐ = 100 kJ/mol.

  1. 3.0 K
  2. 30 K
  3. 13 K
  4. 68 K
Answer and working

B. 30 K

z = 2.303 × 8.314 × 393.15²/100,000 = 30 K. Omitting 2.303 gives 13 K.

Further reading: Singh and Heldman, Introduction to Food Engineering

2 · Chemical and enzyme kinetics in milk systems · hard

Moderately heated milk can show higher plasmin activity in storage than raw milk because heat:

  1. Heat converts β-casein directly into plasminogen in the micelle
  2. Activates lipoprotein lipase, which cleaves casein
  3. Heat destroys the inhibitors first
  4. Removes all plasminogen from the micelles
Answer and working

C. Heat destroys the inhibitors first

Inhibitors of plasmin and of plasminogen activators are more heat-labile than plasminogen and its activators.

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

3 · Protein-protein interactions under heat and pressure · medium

Under high hydrostatic pressure, which whey protein is the most resistant?

  1. β-Lactoglobulin
  2. α-Lactalbumin
  3. Bovine serum albumin
  4. Immunoglobulin G
Answer and working

B. α-Lactalbumin

α-La, with four disulfides and a calcium site, resists to about 400 MPa; β-lg denatures above about 100–200 MPa.

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

4 · Protein-protein interactions under heat and pressure · hard

Alkaline phosphatase cannot be used to verify high-pressure processing of milk because it:

  1. It is destroyed by any pressure above 10 MPa within seconds
  2. Is absent from raw milk
  3. Is produced by pressure-treated bacteria
  4. It survives commercial pressures
Answer and working

D. It survives commercial pressures

Many indigenous enzymes survive pressures that inactivate bacteria.

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

5 · Maillard reaction pathways and advanced glycation products · medium

Furosine in milk is formed:

  1. Naturally in the udder of every cow before milking
  2. From lipid oxidation of fatty acids
  3. From lactose by isomerisation
  4. From Amadori products in acid hydrolysis
Answer and working

D. From Amadori products in acid hydrolysis

It is an analytical artefact used as an index of early Maillard reaction and heat load.

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

6 · Maillard reaction pathways and advanced glycation products · medium

Strecker degradation converts an amino acid into an aldehyde with:

  1. Two more carbons
  2. The same number of carbons and no CO₂
  3. One carbon fewer, plus CO₂
  4. A sugar attached
Answer and working

C. One carbon fewer, plus CO₂

α-Dicarbonyls cause oxidative decarboxylation and deamination: methionine → methional.

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

7 · Mineral equilibria modelling · hard

Mineral equilibrium calculations must be iterative mainly because:

  1. Equilibrium constants change with every repeated measurement
  2. Milk composition is unknown
  3. Ions are not conserved
  4. Ionic strength depends on the speciation being solved
Answer and working

D. Ionic strength depends on the speciation being solved

Speciation changes ionic strength, which changes activities, which changes speciation, until convergence.

Further reading: Holt and others' milk salt models

8 · Proteomics, lipidomics and metabolomics of milk · medium

In bottom-up proteomics of milk, proteins are usually:

  1. Analysed intact by Kjeldahl nitrogen and the 6.38 factor
  2. Trypsin-digested and analysed by LC-MS/MS
  3. Identified by Gerber tests
  4. Separated only by isoelectric precipitation at pH 4.6
Answer and working

B. Trypsin-digested and analysed by LC-MS/MS

Peptides are matched to sequence databases; top-down analyses intact proteins.

Further reading: Proteomics literature

9 · Proteomics, lipidomics and metabolomics of milk · hard

A metabolomics study with 30 samples and 2,000 variables reports perfect separation of two groups by PLS-DA. The main concern is:

  1. Too few variables measured for a multivariate model
  2. NMR cannot be used for milk
  3. Overfitting
  4. PLS-DA cannot classify samples
Answer and working

C. Overfitting

With p ≫ n, chance separation is easy; permutation tests and external validation are needed.

Further reading: Chemometrics literature

10 · Bioactive components and their analysis · medium

Lactoferrin's main antimicrobial mechanism is:

  1. Withholding iron
  2. Hydrolysing peptidoglycan in Gram-positive cell walls
  3. Producing hypothiocyanite
  4. Coagulating casein
Answer and working

A. Withholding iron

Iron sequestration; it also has direct membrane effects. Lysozyme hydrolyses peptidoglycan; lactoperoxidase makes hypothiocyanite.

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

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Read the subject

Advanced Dairy ChemistryThe full study manual, free ICAR AICE-JRF/SRFFormat, sections and how it has changed

More ICAR AICE-JRF/SRF practice

Rheology & Texture of Dairy FoodsFermentation Technology & Dairy BiotechnologyInstrumentation, Process Control & AutomationAdvanced Dairy MicrobiologyAdvanced Dairy Technology & Product DevelopmentAdvanced Dairy EngineeringResearch Methods, Experimental Design & Scientific CommunicationStarter Cultures & Lactic Acid BacteriaDairy Pathogens, Toxins & Microbial RiskQuality Assurance, Statistical Quality Control & Laboratory ManagementDairy Analysis & Instrumental MethodsMicrobiology of Raw & Market MilkChemistry of Dairy ProductsMilk Proteins & EnzymesMicrobiology of Dairy ProductsMembrane Processing & Dairy IngredientsLactose, Milk Salts & VitaminsProbiotics, Prebiotics & Functional Dairy FoodsMicrobiological Quality Assurance & Rapid MethodsDairy Effluent Treatment & Environmental ManagementMilk LipidsEmerging & Non-thermal Dairy ProcessingDairy Plant Utilities & Energy ManagementFermented Milks Technology

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