What is the end product of protein hydrolysis and why

That's all you need to do when composing questions:

1.Acid hydrolysis is commonly used for hydrolysis by H2SO4 or HCl. Disadvantages: Tryptophan is completely broken down, asparagine and glutamine are turned into aspartic acid and glutamic acid. (Proteins are hydrolyzed into amino acids one by one).

2.Alkaline hydrolysis Only tryptophan is stable and everything else is hydrolyzed. If ornithine or urea is present in the hydrolysate, it proves that arginine was present before hydrolysis. (Proteins are hydrolyzed into amino acids one by one).

3.Trypsin hydrolysis breaks only the carboxyl group of lysine or arginine residues to participate in the formation of peptide bonds. If the amino acid sequence is written according to the international standard (i.e., from the N-terminus to the C-terminus), then this enzyme hydrolyzes the peptide bond to the right of the lys or arg that is linked to the next amino acid.

For example, the plot shows that the cleavage site is "|".”asp-lys-|-gly。(Protein cleaves from the break site into a polypeptide).

4.Myrosoptease hydrolysis breaks the carboxy-terminal peptide bonds of hydrophobic amino acid residues of Phe, TRP, and TYR. That is, the peptide bond on the right side of Phe, TRP, and TYR is broken and connected to the next amino acid. (Protein cleaves from the break site into a polypeptide).

5.Thermophilic protease hydrolysis breaks the aminotelopeptide bonds of Leu, Ile (isoleucine), PHE, TRP, VAL, TYR, or MET amino acid residues. That is, the peptide bond of Leu, Ile, Phe, TRP, Val, Tyr, or Met is broken to the left of the previous amino acid.

Generally, this enzyme rarely appears in the questions, and it is almost impossible to test it, unless the teacher wants to deliberately embarrass you. (Protein cleaves from the break site into a polypeptide).

6.Pepsin hydrolysis breaks the peptide bond between two hydrophobic amino acids (PHE, LEU, TRP, TYR). Such as peptide bonds between Phe-Phe, Phe-TRP.

These hydrolases, which are not very specific, are not included in the general exam questions. (Protein cleaves from the break site into a polypeptide).

7.Cyanogen bromide fracture first famous, see clearly, which cyanide of cyanide bromide is, don't look at hydrogen as hydrogen! Only the carboxy-terminal peptide bond of the methionine residue is broken.

The latter sentence is known and known) After the breakage, methionine becomes peptidoyl homoserine lactone. (Protein cleaves from the break site into a polypeptide).

8.Hydroxylamine (NH2OH) cleavage Specifically breaks the peptide bond between ASN-GLY. (Protein cleaves from the break site into a polypeptide).

In fact, some of the enzymes or chemicals above are not only hydrolyzed by the sites I listed, but they are generally not considered during the exam.

Proteins are hydrolyzed at specific sites under the action of enzymes and are used for primary structure and analysis of peptip.

Proteolytic amino acids.

Proteins are destroyed by acid, tryptophan is destroyed, asparagine and glutamine are deamidated groups.

Proteins are under the action of alkalis, and amino acids are racemic after hydrolysis, but tryptophan is stable. Acid hydrolysis due to the subsequent acid pollution to the environment, the hydrolysate products will have peculiar smell; Alkaline hydrolysis will make L-type amino acids become D-type, and there is no specificity between the two hydrolysis methods, so enzymatic hydrolysis has become a trend.

According to the degree of hydrolysis.

1. Complete hydrolysis: The hydrolysate obtained by complete hydrolysis is a mixture of various amino acids.

2. Partial hydrolysis: The hydrolysates obtained by incomplete hydrolysis are peptides of various sizes and individual amino acids.

The end products of protein hydrolysis are a variety of amino acids. The products after protein digestion are CO2 and H2O and urea, and the products after protein combustion are CO2 and H2O oxides and nitrogen, which should be distinguished, protein is hydrolyzed into polypeptides first, and polypeptides are hydrolyzed into final product amino acids, so the final products of protein hydrolysis are various amino acids.

Characteristics of proteolysisProtein hydrolysis occurs under acid or base or protease conditions, the final product of hydrolysis is amino acid, the functional group names in the product are amino and carboxyl groups, the simplest amino acid is called aminoacetic acid, and the structure is simply H2NCH2COOH, so that the reversible coagulation phenomenon of protein is called salting out, and the irreversible coagulation phenomenon is called denaturation.

Protein and starch have a large relative molecular weight, both are polymer compounds, fat is organic matter but the relative molecular weight is small, not a polymer compound, proteolysis breaks the peptide bond, between the broken carbon-oxygen double bond and the carbon-nitrogen single bond, the corresponding amino acid is generated, so the final product of protein hydrolysis is amino acids, the final product of fat hydrolysis is higher fatty acids and glycerol, and the final product of protein hydrolysis is amino acid, containing two functional groups of carboxyl and amino groups.

<> proteolysis refers to the process by which proteolytic enzymes catalyze the hydrolysis of polypeptides or proteins.

Protein hydrolase enzymes are widely distributed in animals, plants and bacteria, and there are many kinds of lysosomes in the digestive tract of animals and various cells in the body.

The content is particularly abundant. Protease.

It plays an important role in the body's metabolism and biological regulation.

The hydrolysis of proteins can be divided into two types: complete hydrolysis and partial hydrolysis according to the degree of hydrolysis

1. Complete hydrolysis, the hydrolysate obtained by the complete hydrolysis of protein is a variety of amino acids.

mixtures; 2. Partial hydrolysis, the hydrolysate obtained by incomplete hydrolysis of protein is a variety of peptides of different sizes and a single amino acid.

The end product of protein hydrolysis is a variety of reluctant-amino acids. The products after protein digestion are CO2, H2O, and urea. The products of protein combustion are oxides of CO2, H2O, and nitrogen.

Protein is hydrolyzed into polypeptides first, and then lead is hydrolyzed into final product amino acids, so the final products of protein hydrolysis are various amino acids. The most desirable end products of protein hydrolysis are a variety of amino acids. The products after protein digestion are CO2, H2O, and urea.

After the protein is burned. The products are oxides of CO2, H2O and nitrogen. Proteins are first hydrolyzed into polypeptides, which are then hydrolyzed into final product amino acids, so the final products of protein hydrolysis are various amino acids.

The end product of protein hydrolysis is a variety of amino acids.

The products after protein digestion are CO2, H2O, and urea.

The products of protein combustion are oxides of CO2, H2O, and nitrogen.

A distinction should be made between the three.