Denaturation of protein result in Loss of its biological activity- Food Science | KATTUFOODTECH

Denaturation of protein – Food Science & Technology Quiz (24-02-2022)

Q1. Denaturation of protein results in ______________.

  1. Loss of its biological activity
  2. Decreased reactivity of constituent groups
  3. Increase in solubility
  4. Resistance to enzymatic hydrolysis

ANSWER: A. Loss of its biological activity

  • Explanation: Denaturation is the breaking of the majority of weak connections or linkages (such as hydrogen bonds) in a protein molecule, which is primarily responsible for the highly organized protein structure in its natural or native state. Denatured proteins have a looser, more random structure and are insoluble in most cases. Denatured proteins, in other words, have lost their biological activity and are no longer capable of performing certain biological roles.

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Q2. Which of the following reactions, commonly, does not depend upon sunlight?

  1. Conversion from ergosterol to cholecalciferol
  2. Rancidity of sesame oils
  3. Protein denaturation
  4. Chlorophyll degradation

ANSWER: C. Protein denaturation

  • Explanation – Protein denaturation is a heat-induced process that does not require sunshine. All of the other processes described in the question are influenced by sunshine exposure. UV radiation, on the other hand, is known to disrupt the functional structure of proteins and is linked to illnesses like cataract formation. This UV radiation can be absorbed by specific amino acids or protein-building components.

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Q3. The attainment of elastic functional properties of protein is mainly due to ___________.

  1. Immobilization
  2. Hydrogen bonding of water
  3. Disulfide crosslinking
  4. Interfacial adsorption

ANSWER – C. Disulfide crosslinking

  • Explanation: Disulfide crosslinks are the mechanism that allows proteins to have elastic functional characteristics. Water absorption, gelation, and foaming functional characteristics of protein are caused by hydrogen bonding, immobilization, and interfacial adsorption. Disulfide linkages that are properly formed give protein stability, reducing unfolded or improperly folded conformations and facilitating folding advancement toward the native state.

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Q4. Which of the following is the structural property of protein?

  1. Emulsification
  2. Coagulation
  3. Cohesion
  4. Gelation

ANSWER: C. Cohesion

  • Explanation: Emulsification, coagulation, and gelation are all examples of surface, enzymatic, and rheological properties of proteins. Protein, on the other hand, has structural qualities like as cohesiveness, elasticity, grittiness, and chewiness. The propensity of like molecules to stick together is known as cohesion. Water has a high degree of cohesiveness (it will form hydrogen bonds).

READ MORE –Food Science & Technology Quiz (24-01-2022)

Q5. The reactive reducing sugars undergo ___________ under heating in case of non-enzymatic browning.

  1. Ring-opening and dehydration
  2. Dehydration and enolization
  3. Enolization and fragmentation
  4. All of the above

ANSWER: D. All of the above

  • Explanation – Under non-enzymatic browning, reactive reducing sugars are responsible for the color and flavor of foods like dates, honey, and chocolate. They suffer ring-opening, enolization, dehydration, and fragmentation as a result of heating. Factors that influence the multiple chemical processes involved have a big impact on the Maillard reaction’s outcome.

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