Amylase
Lipase
Protease
Cellulase
Gluco - Isomerase

Gluco-Oxidase

Transglutaminase
Xylanase
Lactase
Papain
Invertase
Pectinase
Pepsin 

Trypsin
Chymotrypsin
Bromelain
Chymosin
Dextranase
Fructosyl transferase
Inulinase
Serratiopeptidase
Nattokinase

Hemicellulase
Lysozyme
Beta glucanase
Maltase
Phytase
Mucolase
Glutaminase

Mannanase
Alpha-galactocidase

Laccase

Trypsin

(EC No.: 3.4.21.4)

Trypsin enzyme is a kind of protease enzyme of the serine family which catalyzes the breakdown of proteins into smaller peptides. Human to human trypsin differs because of the difference in the climatic condition, and they are responsible for digestion of proteins in the small intestine.

Trypsin enzyme cleaves the peptide bonds from C-terminal end of the lysine and arginine amino acid residue in any reaction.

Functional properties:

• pH: 9.0

• Temperature: 65°C

Some applications of the Trypsin protein:

Food processing:

• Trypsin improves the solubility and gelling properties of food proteins.

• It enhances the digestibility of proteins.

• Helps in reducing the allergens present in the food.

Others:

• It is widely used for protein analytics purposes like protein sequencing.

• In a tissue culture lab for resuspension.

• Used as baking enzyme for dough conditioning

• Enhances the texture and flavor of milk products.

• Used as a meat tenderizer.