Denaturation is the loss of enough structure to render the enzyme inactive | KATTUFOODTECH

Food Science & Technology Quiz (07-06-2022)

Q1. ________ can be defined as the loss of enough structure to render the enzyme inactive.

  1. Denaturation
  2. Proteolysis
  3. Solubility
  4. Stabilization

ANSWER: A. Denaturation

  • Explanation – Denaturation of enzyme proteins can be defined as the loss of enough structure to render the enzyme inactive. Denaturation of enzyme molecules can impact the velocity of the reaction, the affinity for the substrate, the pH optimum, the temperature optimum, the specificity of the reaction, and so on.

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Q2. ________ can be a very sensitive measure of denaturation as some assay procedures are capable of detecting very low levels of product.

  1. Increased proteolysis
  2. Loss of biological activity
  3. Loss of solubility
  4. All of the above

ANSWER: B. Loss of biological activity

  • Explanation – Because some assay protocols may detect extremely low quantities of product, loss of enzymatic activity can be a very sensitive marker of denaturation. In certain circumstances, the loss of activity can be proven to occur only after other structural alterations have been seen using other methods. Before the protein loses its action, it may theoretically be denaturated.

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Q3. ________ measures the wavelength of and the amount of ultraviolet radiation absorbed by a molecule.

  1. UV adsorption spectroscopy
  2. Fluorescence spectroscopy
  3. HPLC
  4. Chromatography

ANSWER – A. UV adsorption spectroscopy

  • Explanation: The wavelength and amount of ultraviolet radiation absorbed by a molecule are measured using ultraviolet adsorption spectroscopy. The wavelength and extent of absorption in proteins are determined by the amino acids present as well as their physical surroundings. Because a protein molecule contains so many of these groups, its UV spectrum is frequently lacking in detail.

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Q4. The interaction of polarized light with protein can be measured by?

  1. Circular dichroism
  2. Optical rotatory dispersion
  3. Fluorescence spectroscopy
  4. Both A and B

ANSWER: D. Both A and B

  • Explanation: Circular dichroism and optical rotatory dispersion techniques can be used to measure the interaction of polarized light with protein. These approaches are used to determine the amount of secondary structure present in proteins, such as alpha-helix, beat sheet, or coil. While these methods do not provide exact estimations of protein secondary structure, they are quite valuable for observing changes. These approaches are extremely sensitive, and even little structural alterations can be identified.

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Q5. The distinct routes are used for the hydrolysis of triacylglycerides (TAG) to free fatty acids (FFA) and glycerol are?

  1. High-pressure steam splitting
  2. Alkaline hydrolysis
  3. Enzymatic hydrolysis
  4. All of the above

ANSWER: D. All of the above

  • Explanation – High-pressure steam splitting, alkaline hydrolysis (saponification), and enzymatic hydrolysis are all employed to convert triacylglycerides (TAG) to free fatty acids (FFA) and glycerol. Fats and oils are hydrolyzed to create free fatty acids, soaps, and glycerol in contemporary industrial processes. Fats and oils are degraded with steam in a countercurrent continuous process at high temperature (250°C) and pressure (50–60 bars) to produce free fatty acids. This is a quick method that produces an aqueous phase with 10% glycerol and an oil phase with 97 percent free fatty acids.

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