Herbivores produce less pepsin because their diets are primarily composed of plant material, which is high in cellulose and requires different digestive enzymes for breakdown. Unlike carnivores, which rely on pepsin to digest proteins from meat, herbivores have evolved specialized digestive systems, including longer intestines and microbial fermentation, to efficiently process plant fibers. Consequently, the need for pepsin is reduced, as their digestion relies more on cellulose-digesting enzymes produced by gut bacteria.
A carnivore organism needs to produce more pepsin because its diet is rich predominently on meat in contrast to a herbivore . The last one contains a lot of proteins for which digestion pepsin plays a crucial role in the digestive system.
Carnivores produce more pepsin than herbivores because they require stronger digestive enzymes to break down protein-rich animal tissues. Pepsin is an enzyme that helps digest proteins in the stomach, and since carnivores consume diets high in protein, they have adapted to produce more of it. In contrast, herbivores primarily consume plant material, which is generally lower in protein and may require different enzymes for digestion, such as cellulase for breaking down cellulose in plant cell walls.
Pepsin is an enzyme that primarily breaks down proteins into smaller peptides in the acidic environment of the stomach. If pepsin were mixed with glucose, there would be no significant reaction, as glucose is a simple sugar and not a protein. Pepsin does not act on carbohydrates, so the glucose would remain unchanged in this mixture. Therefore, the interaction between pepsin and glucose would not produce any meaningful biochemical effect.
Pepsin degrades proteins so if it was active it would immediately begin digesting all the proteins in the cell. Therefore it is produced from a precursor known as a zymogen or proenzyme. Pepsin's proenzyme form is pepsinogen which is transformed to the activated pepsin protein.
No, pepsin is not the substrate in the experiment with BAPNA. BAPNA is the synthetic substrate used in this experiment to test the activity of the enzyme pepsin by measuring the rate of substrate cleavage. Pepsin acts on BAPNA as the enzyme, not the substrate.
A carnivore organism needs to produce more pepsin because its diet is rich predominently on meat in contrast to a herbivore . The last one contains a lot of proteins for which digestion pepsin plays a crucial role in the digestive system.
Carnivores produce more pepsin than herbivores because they require stronger digestive enzymes to break down protein-rich animal tissues. Pepsin is an enzyme that helps digest proteins in the stomach, and since carnivores consume diets high in protein, they have adapted to produce more of it. In contrast, herbivores primarily consume plant material, which is generally lower in protein and may require different enzymes for digestion, such as cellulase for breaking down cellulose in plant cell walls.
Well using less pepsin means you have less of the enzyme. Now if you keep the substrate / enzyme ratio constant there won't be anything changing. If you however decrease the pepsin amount, there will be less active sites for the same amount of substrate to bind. ---> slower reaction
enzymes
Gastrugy produce pepsin and renin pepsin help to decompose protein food why renin help to decompose milk for more information send it to my mail samueljackson626@Yahoo.com
Pepsin is the powerful enzyme in gastric juice that digests proteins such as those in meat, eggs, seeds, or dairy products in the stomach. Since animals have stomachs, they therefore have pepsin.
pepsin
Pepsin
Pepsin is an enzyme that primarily breaks down proteins into smaller peptides in the acidic environment of the stomach. If pepsin were mixed with glucose, there would be no significant reaction, as glucose is a simple sugar and not a protein. Pepsin does not act on carbohydrates, so the glucose would remain unchanged in this mixture. Therefore, the interaction between pepsin and glucose would not produce any meaningful biochemical effect.
Yes. The precursor of pepsin is called pepsinogen; it is produced by stomach cells and then activated by the HCl in the stomach. Pepsin works best at very low pH.... e.g. acid conditions of the stomach. The small intestine has glands that produce neutralize the acid. Pepsin denatures at pH's of 5,0 or higher..... so effectively it is neutralized when the chyme enters the small intestine.
Yes, Bumblebees eat nectar which is plant produce
The inactive precursor of pepsin is called pepsinogen. It is secreted by the gastric chief cells in the stomach lining and is activated to pepsin in the presence of hydrochloric acid (HCl) in the gastric environment. This activation process prevents the enzyme from digesting the proteins in the cells that produce it. Pepsin then plays a crucial role in protein digestion by breaking down complex proteins into smaller peptides.