Abstract
Crude preparations of extracellular cellulase and xylanase from Cellulomonasflavigena at 4°C show a rapid loss of activity. With the protease inhibitors aprotinin and α-2 macroglobulin this loss of activity could be dramatically reduced. Cellulase and xylanase extracted from a protease negative mutant were also more stable. When the cellulase and xylanase was purified by DEAE sepharose from wild type strains, the protease activity could be separated, such preparations of cellulase and xylanase were extremely stable.
Original language | English |
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Pages (from-to) | 891-894 |
Number of pages | 4 |
Journal | Biotechnology Letters |
Volume | 11 |
Issue number | 12 |
DOIs | |
Publication status | Published - Dec 1989 |