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Q: The enzyme used in all experiments in this lab was pepsin?
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What effect does freezing have on pepsin activity?

Heat affect any enzyme and so pepsin. A temperature about 80 degrees can degarade most of the proteins and pepsin. At this temperature pepsin loose its structure and can not be active after that.


The official ending of all enzyme names?

ase.Synthase, as exampleStill, not all enzymes have this ending. In the old days there were no naming rules. Pepsin, a digestive enzyme, is an example of non-naming by the modern rules.


How pepsin inactivated?

Pepsin is a digestive enzyme found in our digestive system for protein degradation.Pepsin can be irreversibly denatured at alkaline pH (pH 8.5 - 11) at room temperature. It can also be denatured by boiling at above 81 degree Celsius. The degraded form of protein is catalytically dead afterwards.


Why can pepsin not be produced in its active form?

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.


Does chymotrypsin digest proteins?

Yes, chymotrypsin digests proteins. Chymotrypsin is included in the group of proteolytic enzymes called "serine proteases". This name is referred to their common catalytic mechanism characterized by a particular reactive Serine residue that is essential for their enzymatic activity. Chymotrypsin is secreted from the pancreas and has a particular breakage activity of peptide bond from proteins. To do this, the protein to be digested has to have a Phenylalanine (Phe), Tryptophan (Trp), or a Tyrosine (Tyr) as bulky amino acid residues before the peptide bond to be cleaved. Moreover, when that particular amino acid residue, just before the peptide bond, is an Asparagine (Asn), Histidine (His), Methionine (Met) or Leucine (Leu), the breakage process is slower. Finally, when the amino acid residue previous to the peptide bond is a Proline (Pro), the cleavage doesn't take place.

Related questions

Which digestive organs produces pepsin?

Pepsin is an enzyme in the stomach that begins the digestion of proteins by splitting them into smaller pieces. It is a gastric protease; pepsin is secreted in an inactive form, pepsinogen, which is activated by stomach acid. enzyme produced in the mucosal lining of the stomach that acts to degrade protein.


What effect does freezing have on pepsin activity?

Heat affect any enzyme and so pepsin. A temperature about 80 degrees can degarade most of the proteins and pepsin. At this temperature pepsin loose its structure and can not be active after that.


Is pepsinogen organic or inorganic?

Pepsinogen is an inactive form of the digestive enzyme pepsin. Almost all enzymes are proteins, and proteins are organic macromolecules.


What is the most important enzyme in gastric juice?

Pepsin is the most important enzyme in gastric juice. It begins the digestion of nearly all types of dietary protein into polypeptides. (Originates from the inactive form pepsinogen)


Who used experiments?

we are all scientists. we all use experiments


The official ending of all enzyme names?

ase.Synthase, as exampleStill, not all enzymes have this ending. In the old days there were no naming rules. Pepsin, a digestive enzyme, is an example of non-naming by the modern rules.


What enzyme speeds up the breakdown of food?

It varies for all the food groups. For fat/lipid lipase breaks down,for proteins pepsin breaks down and for carbohydrates amylase.


What are the Enzyme reactions in the stomach?

Pepsin, Hydrochloric acid. First one is enzyme deals with proteins (meat for example). All in the stomach.They all in one is called gastric juice. Gastric juice is responsible for breaking down foods you eat so digestion can continue in the small intestine.


What is needed for the stomach protein digesting enzymes to become active?

Zymogens are stored in their inactive form and need the Hydrochloric acid (or HCl) to be activated. Specifically, HCl converts pepsinogen into pepsin which can then be used to convert more pepsinogen into pepsin.


What does pepsin digest?

the pepsin help the protein to digest and breaks into polypeptides


How pepsin inactivated?

Pepsin is a digestive enzyme found in our digestive system for protein degradation.Pepsin can be irreversibly denatured at alkaline pH (pH 8.5 - 11) at room temperature. It can also be denatured by boiling at above 81 degree Celsius. The degraded form of protein is catalytically dead afterwards.


What makes enzymes in the digestive system?

first salivary glands in the mouth which produce an enzyme which help in digesting carbohydrates. second gastric gland in stomach produce an enzyme called pepsin which help in digesting protein third in the pancreas which produce the three types of enzymes that digest all types of food .