Chymotrypsin A

Chymotrypsin (Chymotrypsin A) is a serine protease synthesized by the pancreas, which cleaves protein chains on the carboxyl side of aromatic amino acids.

Trypsin-Chymotrypsin 6:1 is a biocatalyst and a key enzyme in new biocatalyst technology. Enzyme engineering focuses on improving reaction kinetics, substrate selectivity, and activity under extreme conditions (e.g., low or high pH). Introducing stimulus-responsive modifications to these enzymes also enables dynamic activity control.

Trypsin-Chymotrypsin 1:1 is a biocatalyst and a pivotal enzyme in new biocatalytic technology. Enzyme engineering focuses on improving enzyme reaction kinetics, substrate selectivity, and activity under extreme conditions (e.g., low or high pH). By introducing stimulus responsiveness into these enzyme modifications, dynamic control of activity is also achievable.

Trypsin-Chymotrypsin 1:250 is a biocatalyst, and a crucial enzyme in new biocatalyst technology. Enzyme engineering focuses on improving enzyme reaction kinetics, substrate selectivity, and activity under harsh conditions (e.g., low or high pH). By incorporating stimulus-responsive modifications into these enzymes, dynamic control of activity has also become feasible.

TLCK-treated Chymotrypsin is a type of serine protease that cleaves protein chains at the carboxyl side of aromatic amino acids. It undergoes TLCK treatment to inactivate residual trypsin activity.

5-Bromo-4-chloro-1H-indol-3-yl nonanoate is a fluorescent substrate used for enzyme detection. It reacts with various enzymes to produce fluorescent products and has demonstrated activity with β-galactosidase, α-chymotrypsin, and β-glucuronidase.