Q1. Pea protein is roughly ______ vicilin and 28% legumin.

1. 23%
2. 43%
3. 33%
4. 53%

ANSWER: B. 43%

• Explanation: Pea protein is roughly 43% vicilin and 28% legumin. In comparison to cereal grains and some other pulses, the common pea (Pisum savitum L.) has a macronutrient composition that is high in protein and fiber. The pea contains four Osborne protein classes: globulin (55-65%), albumin (18-25%), a prolamin (4-5%), and glutelin (4-5%). (3-4 percent ). Pea’s functional qualities are crucial due to its high concentration of globulin proteins. The protein that is also significant in soy texturization is found in the globulin fraction. Two particular globulin proteins, vicilin, and legumin are found in the globulin fraction of pea. Pea protein is made up of around 43% vicilin and 28% legumin.

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Q2. Pea protein also contains _______ which is absent in other legumes.

1. Globulin
2. Convicilin
3. Vicillin
4. Prolamin

ANSWER: B. Convicilin

• Explanation – Convicilin, which is missing in other legumes, is also found in pea protein. This storage protein has a higher sulfur content than vicilin. Pea protein may be effective in textured plant protein applications due to the role of disulfide bonds in the synthesis of fibers in TVP and the presence of methionine in the legumin fraction. While the rate at which pea protein is heated does not affect gelling, the rate at which it is cooled does, and legumin protein has a stronger gel when chilled at a slower rate.

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Q3. _________ is a test that determines properties of polymers such as starch gelatinization and protein denaturation temperatures through heat flow changes

1. Swelling power
2. DSC
3. Least gelation concentration
4. None of the above

ANSWER – B. DSC

• Explanation: Differential Scanning  Calorimetry is a thermal analysis technique that uses heat flow changes to assess properties of polymers such as starch gelatinization and protein denaturation temperatures. Because of the amount of energy required to denature a bond, knowing its thermal denaturation properties can assist assess its strength. A higher denaturation temperature for proteins indicates greater heat stability. This can also be used to detect how much denaturation has occurred in commercial protein isolates.

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Q4. _____ is the concentration of protein at which a strong gel is formed with the addition of water and heat, followed by cooling.

1. Gelatinization
2. Retrogradation
3. Least gelation concentration(LGC)
4. Both B and C

ANSWER: C. Least gelation concentration(LGC)

• Explanation:  For TVP, the creation of protein networks is crucial, and gelling is one measure of a protein’s capacity to texturize properly. With the addition of water and heat, followed by cooling, LGC is the protein concentration at which a strong gel is created. Protein extraction techniques can have a big impact on gelation concentration, hence extracted proteins from the same source can have different gelation concentrations. Because of the stronger gelling structure, a lower gelation concentration may produce a better-textured result.

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Q5. ________ has been used for understanding the functionality of starch-based raw materials in extrusion applications, but its use for studying transitions related to material flow and viscosity in proteins is unique.

1. Rapid Visco analyzer
2. Phase transition analysis(PTA)
3. GC-MS
4. Texture profile analysis

ANSWER: B. Phase transition analysis(PTA)

• Explanation – PTA had previously been used to investigate the functionality of starch-based raw materials in extrusion applications, but it is the first time it has been utilized to study transitions in protein material flow and viscosity. A tiny amount of hydrated sample (1.5-2.5 g) is compressed in a test chamber at pressures up to 100 bars and heated at a steady pace from 5-7°C to 120°C or higher until the material starts to flow out of a capillary at the bottom of the chamber for PTA analysis. The flow temperature (Tf) is an indirect measure of viscosity or resistance to flow.

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