Trypsin Agarose

The trypsin molecule has two domains: one is related to the enzyme active site and the tryptophan residues; the other is related to the 8-anilinonaphthalene-1-sulfonate binding.

Trypsin Agarose is an insoluble enzyme product. It is produced by reacting a conventional "soluble" enzyme (trypsin) with an inert base (agarose). This insoluble conjugate retains the activity of the original enzyme. Trypsin bound to agarose are highly stable and maintain denaturing conditions for longer time than the soluble trypsin.

A very active and very stable trypsin agarose derivative has been used to optimize the design of the synthesis of a model dipeptide, benzoylarginine leucinamide. Trypsin has also been used in a study to investigate protonation-state determination in proteins using high-resolution X-ray crystallography.

Trypsin Agarose has been used for enzymatic hydrolysis of prolamins and gliadin to generate peptides.

Insolubilized

One unit will hydrolyze 1.0 μmole of BAEE per min at pH 8.0 at 30 °C (titrimetric assay).

Suspension in approx. 10 mM acetic acid, pH 3.2