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

The Food Biotechnology, Biochemistry & Nutrition syllabus for CFTRI M.Sc. (Food Technology) in full: 3 chapters and 11 topics, every one listed below, plus 53 Food Biotechnology, Biochemistry & Nutrition flashcards with answers.

3Chapters
11Topics
53Flashcards

Food Biotechnology, Biochemistry & Nutrition syllabus: all 3 chapters

Expand any chapter to see its topics and sub-topics.

  1. Cell Biology

    3 topics
    • Molecular Biology
    • Enzymes, Coenzymes and Cofactors
    • Hormones
  2. Metabolism

    4 topics
    • Carbohydrate Metabolism
    • Fat Metabolism
    • Protein Metabolism
    • Photosynthesis
  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

CFTRI M.Sc. (Food Technology) Food Biotechnology, Biochemistry & Nutrition flashcards — 53 questions with 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.

Show the other 33 Food Biotechnology, Biochemistry & Nutrition flashcards
  1. What is the function of the pentose phosphate pathway?

    It generates NADPH for biosynthesis (e.g., fatty acid synthesis) and ribose-5-phosphate for nucleotide synthesis, operating in the cytoplasm parallel to glycolysis.

  2. What is beta-oxidation and where does it occur?

    Beta-oxidation is the mitochondrial breakdown of fatty acids into acetyl-CoA units, each cycle removing 2 carbons and yielding 1 FADH2, 1 NADH, and 1 acetyl-CoA.

  3. Why do fats yield more energy per gram than carbohydrates?

    Fatty acids are more highly reduced (more C-H bonds) and contain less oxygen, so their oxidation releases more energy; fat gives about 9 kcal/g versus 4 kcal/g for carbohydrate.

  4. What are ketone bodies, when are they formed, and name them.

    Ketone bodies (acetoacetate, beta-hydroxybutyrate, acetone) are made in the liver from excess acetyl-CoA during starvation, fasting, or uncontrolled diabetes, and serve as fuel for brain and muscle.

  5. Where does fatty acid synthesis occur and what is the key precursor and reducing agent?

    Fatty acid synthesis occurs in the cytoplasm using acetyl-CoA (via malonyl-CoA) as building blocks and NADPH as the reducing agent, catalyzed by fatty acid synthase.

  6. Distinguish saturated, monounsaturated, and polyunsaturated fatty acids.

    Saturated fatty acids have no C=C double bonds; monounsaturated have one double bond; polyunsaturated have two or more double bonds (e.g., omega-3, omega-6).

  7. What are essential fatty acids and give examples?

    Fatty acids the body cannot synthesize and must obtain from diet: linoleic acid (omega-6) and alpha-linolenic acid (omega-3).

  8. What is transamination in protein metabolism?

    The transfer of an amino group from an amino acid to a keto acid (usually alpha-ketoglutarate), catalyzed by transaminases using pyridoxal phosphate (vitamin B6) as coenzyme.

  9. What is the urea cycle and why is it important?

    It is the liver pathway that converts toxic ammonia (from amino acid catabolism) into urea for excretion; it detoxifies nitrogenous waste and occurs partly in mitochondria and partly in the cytoplasm.

  10. Distinguish essential from non-essential amino acids and give examples.

    Essential amino acids must come from the diet (e.g., lysine, leucine, valine, methionine, tryptophan); non-essential amino acids can be synthesized by the body (e.g., alanine, glutamate, glycine).

  11. What does nitrogen balance indicate in protein nutrition?

    It compares nitrogen intake to excretion: positive balance (growth, pregnancy) means intake exceeds loss; negative balance (starvation, illness) means loss exceeds intake; zero balance is maintenance in healthy adults.

  12. Write the overall balanced equation for photosynthesis.

    6 CO2 + 6 H2O + light energy -> C6H12O6 + 6 O2 (carbon dioxide and water converted to glucose and oxygen using light energy).

  13. What are the two stages of photosynthesis and where does each occur?

    The light-dependent reactions occur in the thylakoid membranes (produce ATP, NADPH, O2); the light-independent reactions (Calvin cycle) occur in the stroma (fix CO2 into glucose).

  14. What is the role of chlorophyll in photosynthesis?

    Chlorophyll is the green pigment in chloroplasts that absorbs light energy (mainly red and blue, reflecting green) to drive the light reactions; chlorophyll-a is the primary pigment.

  15. What enzyme catalyzes CO2 fixation in the Calvin cycle and what is the first stable product in C3 plants?

    RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) fixes CO2; the first stable product in C3 plants is 3-phosphoglycerate (3-PGA), a 3-carbon compound.

  16. Classify vitamins into the two solubility groups with examples.

    Fat-soluble vitamins: A, D, E, K (stored in body fat). Water-soluble vitamins: B-complex and C (not stored, needed regularly).

  17. Match these deficiency diseases to their vitamins: scurvy, rickets, beriberi, pellagra.

    Scurvy - vitamin C; rickets - vitamin D; beriberi - thiamine (B1); pellagra - niacin (B3).

  18. What is the main function of vitamin A and what deficiency does it cause?

    Vitamin A (retinol) is essential for vision (forms rhodopsin), epithelial integrity, and immunity; deficiency causes night blindness and xerophthalmia.

  19. What is the function of vitamin K and vitamin D in the body?

    Vitamin K is required for blood clotting (synthesis of clotting factors); vitamin D promotes intestinal calcium and phosphorus absorption for bone mineralization.

  20. Which vitamin functions as a major water-soluble antioxidant and aids iron absorption?

    Vitamin C (ascorbic acid); it is also required for collagen synthesis and enhances absorption of non-heme iron.

  21. What deficiency disease is caused by lack of vitamin B12 and folate?

    Megaloblastic (pernicious) anemia; both are needed for DNA synthesis and red blood cell maturation, and B12 deficiency also causes neurological damage.

  22. Distinguish macrominerals from microminerals (trace elements) with examples.

    Macrominerals are needed in larger amounts (calcium, phosphorus, sodium, potassium, magnesium); microminerals/trace elements are needed in tiny amounts (iron, zinc, iodine, copper, selenium).

  23. What are the main functions of calcium and iron in the body?

    Calcium: bone and teeth formation, blood clotting, muscle contraction, nerve function. Iron: component of hemoglobin and myoglobin for oxygen transport; deficiency causes anemia.

  24. What is the role of sodium and potassium in the body?

    They are the major electrolytes maintaining fluid balance, osmotic pressure, and nerve/muscle excitability; sodium is mainly extracellular and potassium mainly intracellular (sodium-potassium pump).

  25. Which mineral is essential for thyroid hormones and which deficiency disease results?

    Iodine is required for thyroxine (T4) and T3; deficiency causes goiter and, in children, cretinism.

  26. What is the structural difference between DNA and RNA?

    DNA has deoxyribose sugar, the base thymine, and is usually double-stranded; RNA has ribose sugar, the base uracil, and is usually single-stranded.

  27. Name the three main types of RNA and their functions.

    mRNA carries the genetic code from DNA to ribosomes; tRNA brings amino acids to the ribosome during translation; rRNA forms the structural and catalytic core of ribosomes.

  28. What are nucleotides composed of?

    Each nucleotide has three parts: a nitrogenous base (purine or pyrimidine), a pentose sugar (ribose or deoxyribose), and one or more phosphate groups.

  29. Besides heredity, name two important roles of nucleotides in metabolism.

    ATP/GTP serve as energy currency; nucleotides also form coenzymes (NAD, FAD, coenzyme A) and act as signaling molecules (cyclic AMP).

  30. What is the physiological caloric value (Atwater factors) of carbohydrates, proteins, and fats?

    Carbohydrates and proteins yield about 4 kcal/g each; fats yield about 9 kcal/g; (alcohol yields about 7 kcal/g).

  31. What is Basal Metabolic Rate (BMR) and how is Body Mass Index (BMI) calculated?

    BMR is the energy expended at complete rest to maintain vital functions; BMI = weight(kg) / height(m)^2, used to classify underweight, normal, overweight, and obese.

  32. What is dietary fiber and why is it important for health?

    Dietary fiber is indigestible plant carbohydrate (cellulose, pectin, etc.); it aids bowel movement, lowers cholesterol, controls blood sugar, and gives satiety though it provides little energy.

  33. Define a balanced diet.

    A diet that provides all nutrients (carbohydrates, proteins, fats, vitamins, minerals, water, and fiber) in correct proportions and adequate amounts to meet the body's needs for energy, growth, and maintenance.

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

What is in the CFTRI M.Sc. (Food Technology) Food Biotechnology, Biochemistry & Nutrition syllabus?

CFTRI M.Sc. (Food Technology) Food Biotechnology, Biochemistry & Nutrition is split into 3 chapters: Cell Biology, Metabolism and Nutrition. Together they contain 11 topics.

How many chapters are in CFTRI M.Sc. (Food Technology) Food Biotechnology, Biochemistry & Nutrition?

3 chapters, containing 11 topics. The largest chapter is Metabolism, with 4 topics.

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

Yes — a 53-card Food Biotechnology, Biochemistry & Nutrition deck, printed in full in the flashcards section of this page and available in the Examius app with spaced repetition. The free plan covers one exam of your choice, including its flashcards; Examius Pro, a one-time purchase, unlocks every other exam and deck.