Chymotrypsin is a proteolytic enzyme, which preferentially catalyzes the hydrolysis of peptide bonds involving L-isomers of tyrosine, phenylalanine and tryptophan. The optimum pH is 8.0. The enzyme is inhibited by heavy metals, the natural trypsin inhibitors to various degrees.
The ultrapure Chymotrypsin has been further purified by affinity chromatography to remove trace contaminating proteases.
TESTING ITEM S | SPECIFICATIONS | RESULTS |
APPEARANCE | WHITE POWDER | WHITE POWDER |
MICROBIAL LIMITS | --- | --- |
PSEUDOMONAS AERUGINOSA | NEGATIVE | NEGATIVE |
SALMONELLA SPECIES | NEGATIVE | NEGATIVE |
STAPHYLOCOCCUS AUREUS | NEGATIVE | NEGATIVE |
LOSS ON DRYING | NOT MORE THAN 5.0% | 0.9% |
RESIDUE ON IGNITION | NOT MORE THAN 2.5% | 0.2% |
LIMIT OF TRYPSIN | NOT MORE THAN 1% | COMPLIED |
ACTIVITY | NOT LESS THAN 1000USP UNITS/MG,CALCULATED ON THE DRIED BASIS | 1052USP UNITS/MG |
