Affinity process for trypsin purification and stabilization

Details Affinity process for trypsin purification and stabilization Affinity process for trypsin purification and stabilization

1988-02-26

1990-11-27

Schain, Howard E.

Chemistry: molecular biology and microbiology

Enzyme , proenzyme; compositions thereof; process for...

Hydrolase

530413, C12N 976

Patent

active

049735543

ABSTRACT:
A water soluble ligand bound polymer has been synthesized and used for purification and stabilization of trypsin, an easily autodigestible enzyme. The affinity polymer was formed by copolymerizing N-acryloyl-m-amino-benzamidine, and acrylamide in the absence of oxygen. Bound trypsin could be easily eluted by either arginine or benzamidine. At low temperature (<5.degree. C.), the polymer solution was very stable and retained its high capacity for trypsin binding after 6 months of storage. Trypsin can also be stored in this system for extended periods. Combining the principles of affinity chromatography and ultrafiltration, a process has been developed, using this polymer, for purification of trypsin. The purification process also features provisions for the recirculation of the eluant as well as the macroligand.

REFERENCES:
patent: 4350760 (1982-09-01), Nicolas
Annals of N.Y. Acad. of Sci. 369,257-263 (1981), Schneider.
J. of Membrane Science, 9, 337-342 (1981), Adamski-Medda.
Annals of N.Y. Acad. of Sci. 413, 307-309 (1983), Mattiasson.
Biotechnology Letters, vol. 8, No. 3, 163-168 (1986), Choe.

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