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Trypsin is a digestive enzyme that cleaves peptide bonds (a serine protease). It cuts proteins only at carboxyl side of lysine and arginine residues (endopeptidase) by hydrolysis. Aspartate (Asp 189) residue located in the catalytic pocket (S1) of trypsin is responsible for attracting and stabilizing positively-charged lysine and/or arginine. The optimum pH for Trypsin is 8.
Trypsin(EC 3.4.21.4) family of serine proteases are enzymes that cleave prot ...

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