Purification of elastase-like chymotrypsin from cardamom shoot and capsule bore

Abstract

An elastase-like chymotrypsin was purified by aprotinin-agarose affinity chromatography from the midgut extract of cardamom shoot and capsule borer, Conogethes punctiferalis. The purified enzyme had a V-max of 687.6 +/- 22.1 nmole pNA released/min/mg protein, K-m of 0.168 +/- 0.012 mM with SAAPLpNA as substrate and gave a single band on SDS-PAGE with a molecular mass of 72.1 kDa. Casein zymogram revealed one clear zone of proteolytic activity, which corresponded to the band obtained with SDS-PAGE indicating that this could be a single-polypeptide enzyme

Published in

Indian Journal of Experimental Biology
2007, Volume: 45, number: 11, pages: 998-1002 Publisher: NATL INST SCIENCE COMMUNICATION

UKÄ Subject classification

Food Science
Agricultural Science
Environmental Sciences related to Agriculture and Land-use

Permanent link to this page (URI)

https://res.slu.se/id/publ/16340