CelA from Bacillus lautus PL236 Encodes a Novel Cellulose-Binding Endo-(Beta)-1, 4-Glucanase
In a study, EG-A-L and EG-A-S were purified to homogenity and shown to have almost identical characteristics with respect to activity against soluble substrates and pH and temperature dependency. EG-A-L binds strongly to cellulose, in contrast to EG-A-S, and has higher activity against insoluble sub...
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Veröffentlicht in: | Journal of bacteriology 1992-06, Vol.174 (11), p.3522 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | In a study, EG-A-L and EG-A-S were purified to homogenity and shown to have almost identical characteristics with respect to activity against soluble substrates and pH and temperature dependency. EG-A-L binds strongly to cellulose, in contrast to EG-A-S, and has higher activity against insoluble substrates than the latter. |
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ISSN: | 0021-9193 1098-5530 |