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
Hauptverfasser: Hansen, Christian K, Diderichsen, Borge, Jorgensen, Per L
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.
ISSN:0021-9193
1098-5530