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.
Keywords
aprotinin; cardamom; chymotrypsin; Conogethes punctiferalis; trypsin
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 and Nature Conservation
Permanent link to this page (URI)
https://res.slu.se/id/publ/16340