CFTRI M.Sc. (Food Technology) Food Biotechnology, Biochemistry & Nutrition Syllabus

Food Biotechnology, Biochemistry & Nutrition syllabus — full chapter and topic list

Expand any chapter to see its topics and sub-topics. This is the whole examinable outline for Food Biotechnology, Biochemistry & Nutrition in CFTRI M.Sc. (Food Technology), not a summary of it.

1. 1

   Cell Biology

   3 topics

   • Molecular Biology
   • Enzymes, Coenzymes and Cofactors
   • Hormones
2. 2

   Metabolism

   4 topics

   • Carbohydrate Metabolism
   • Fat Metabolism
   • Protein Metabolism
   • Photosynthesis
3. 3

   Nutrition

   4 topics

   • Vitamins and their Function in the Body
   • Minerals and their Function in the Body
   • Nucleic Acids and their Importance
   • Food and Health

Food Biotechnology, Biochemistry & Nutrition flashcards for CFTRI M.Sc. (Food Technology)

20 of 53 cards from the Food Biotechnology, Biochemistry & Nutrition deck — real questions with worked answers.

1. What is the Central Dogma of molecular biology?

   The unidirectional flow of genetic information: DNA -> RNA -> Protein, via transcription (DNA to RNA) and translation (RNA to protein); reverse transcription (RNA to DNA) is an exception.

2. In DNA, which bases pair with each other and by how many hydrogen bonds?

   Adenine pairs with Thymine via 2 hydrogen bonds; Guanine pairs with Cytosine via 3 hydrogen bonds (in RNA, Thymine is replaced by Uracil).

3. What does Chargaff's rule state about DNA base composition?

   In double-stranded DNA, the amount of adenine equals thymine (A = T) and guanine equals cytosine (G = C); thus purines equal pyrimidines (A+G = T+C).

4. What type of DNA replication occurs in cells and what does the term mean?

   Semiconservative replication: each new DNA double helix contains one parental (old) strand and one newly synthesized strand, demonstrated by the Meselson-Stahl experiment.

5. What is the role of a promoter and a codon in gene expression?

   A promoter is the DNA region where RNA polymerase binds to initiate transcription; a codon is a triplet of mRNA nucleotides that specifies a particular amino acid during translation.

6. Define an enzyme and the type of molecule most enzymes are.

   An enzyme is a biological catalyst that speeds up reactions by lowering activation energy without being consumed; most enzymes are proteins (some are catalytic RNA called ribozymes).

7. Distinguish between a coenzyme, a cofactor, and an apoenzyme.

   A cofactor is a non-protein helper (often a metal ion) needed for enzyme activity; a coenzyme is an organic cofactor (often vitamin-derived); an apoenzyme is the inactive protein part without its cofactor (apoenzyme + cofactor = holoenzyme).

8. According to the IUBMB system, what are the six main classes of enzymes?

   Oxidoreductases, Transferases, Hydrolases, Lyases, Isomerases, and Ligases.

9. What do Km and Vmax represent in the Michaelis-Menten equation?

   Vmax is the maximum reaction rate at saturating substrate; Km (Michaelis constant) is the substrate concentration at half Vmax and indicates enzyme-substrate affinity (low Km = high affinity).

10. How does competitive inhibition differ from non-competitive inhibition in terms of Km and Vmax?

    Competitive inhibition increases apparent Km but leaves Vmax unchanged (inhibitor competes at the active site); non-competitive inhibition decreases Vmax but leaves Km unchanged (inhibitor binds elsewhere).

11. Name three coenzymes derived from B-vitamins and their parent vitamins.

    NAD+/NADP+ from niacin (B3); FAD/FMN from riboflavin (B2); coenzyme A from pantothenic acid (B5); TPP from thiamine (B1); pyridoxal phosphate from B6.

12. What is a hormone and what are the two major chemical classes?

    A hormone is a chemical messenger secreted by endocrine glands into the blood to regulate target tissues; major classes are steroid hormones (lipid-derived) and peptide/protein and amino-acid-derived hormones.

13. Which hormones regulate blood glucose and what are their opposing actions?

    Insulin lowers blood glucose (promotes uptake and glycogen synthesis); glucagon raises blood glucose (promotes glycogenolysis and gluconeogenesis). Both are secreted by the pancreas.

14. Which thyroid hormones are produced and what mineral is essential for their synthesis?

    Thyroxine (T4) and triiodothyronine (T3); iodine is essential, and deficiency causes goiter and hypothyroidism.

15. What is the difference in mechanism between steroid and peptide hormones?

    Steroid hormones are lipid-soluble, cross the cell membrane, and bind intracellular receptors to affect gene transcription; peptide hormones are water-soluble, bind surface receptors, and act via second messengers like cAMP.

16. What is glycolysis, where does it occur, and what is its net ATP yield?

    Glycolysis is the breakdown of one glucose (6C) into two pyruvate (3C) in the cytoplasm; net yield is 2 ATP and 2 NADH per glucose.

17. What is the net ATP yield from complete aerobic oxidation of one glucose molecule?

    About 30-32 ATP (older texts cite 36-38), produced via glycolysis, the citric acid cycle, and oxidative phosphorylation.

18. What is the citric acid (Krebs) cycle and where does it occur?

    It is the cyclic oxidation of acetyl-CoA to CO2 in the mitochondrial matrix, producing per acetyl-CoA: 3 NADH, 1 FADH2, 1 GTP (ATP), and 2 CO2.

19. Define glycogenesis, glycogenolysis, and gluconeogenesis.

    Glycogenesis is glycogen synthesis from glucose; glycogenolysis is glycogen breakdown to glucose; gluconeogenesis is synthesis of glucose from non-carbohydrate sources (amino acids, lactate, glycerol).

20. What is the Cori cycle?

    The cycle in which lactate produced by anaerobic glycolysis in muscle is transported to the liver, converted back to glucose via gluconeogenesis, and returned to muscle.

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