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 degreesC 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 3...
Main Authors: | , , , |
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Format: | Article in Journal/Newspaper |
Language: | Spanish |
Published: |
KLUWER ACADEMIC PUBL
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Subjects: | |
Online Access: | http://hdl.handle.net/10533/197643 https://doi.org/10.1023/A:1016383212244 |
Summary: | The isolation and preliminary characterization of a trypsin-like protease with high activity at 20 degreesC 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 degreesC on BAPNA is 0.5 U/mg. |
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