Isolation, purification and preliminary characterization of cryophilic proteases of marine origin.
The isolation and preliminary characterization of a trypsin-like protease with high activity at 20 degrees C is described. This protease was isolated from Antarctic krill (Euphasia superba) by a two-step chromatography process and the use of zymogram analyses. The protease has a molecular weight of 30 kDa and a pI of 4.1. Its specific activity at 20 degrees C on BAPNA is 0.5 U/mg.
Salamanca
M H
MH
Center for Biochemical Engineering and Biotechnology, Department of Chemical Engineering, University of Chile, Santiago.
Barría
C
C
Asenjo
J A
JA
Andrews
B A
BA
D000818:Animals; D001586:Benzoylarginine Nitroanilide; D002847:Chromatography, Agarose / Q000379:methods; D003445:Crustacea / Q000201:enzymology*; D010450:Endopeptidases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D007526:Isoelectric Point; D008970:Molecular Weight; D013379:Substrate Specificity
D001586:Benzoylarginine Nitroanilide; D010450:Endopeptidases