A novel bovine trypsin isoform was purified from commercial sample by ion exchange chromatography by Sephadex SP C50®. New isoform contains in addition of loss of N-terminus hexapeptide (as found in parent molecule β-trypsin) an intra-chain split between Lys-155 and Ser-156. The novel enzyme denominate γ-trypsin showed similar properties with α-trypsin isoform in polypeptide number chain (two chain), molecular masses (23,312 Da), secondary structure, hydrodynamic radius and others. In spite of enzymatic and structural similarities of both isoforms, γ-trypsin preferably has a lower rate formation from β-trypsin, a lower surface charge, but the γ-trypsin has a higher thermal stability than α-trypsin. Due to obtaining facility of purification of bovine trypsin isoforms from commercial font, and properties described above, this enzyme becomes an interesting alternative for the food industry, detergent and biocatalysis research.
Keywords: Enzymatic activity; Physicochemical; Protein stability; Trypsin isoforms; γ-Trypsin.
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