DOI | Trouver le DOI : https://doi.org/10.1007/BF00175740 |
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Auteur | Rechercher : Gilbert, M.; Rechercher : Yaguchi, M.1; Rechercher : Watson, D. C.1; Rechercher : Wong, K. K. Y.; Rechercher : Breuil, C.; Rechercher : Saddler, J. N. |
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Affiliation | - Conseil national de recherches du Canada. Institut des sciences biologiques du CNRC
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Format | Texte, Article |
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Résumé | Two thermophilic xylanases (xylanase II from Thielavia terrestris 255B and the 32-kDa xylanase from Thermoascus crustaceus 235E) were studied to determine if they had different and complementary modes of action when they hydrolysed various types of xylans. Partial amino acid sequencing showed that these two enzymes belonged to different families of β-1,4-glycanases. Xylanase II achieved faster solubilization of insoluble xylan whereas the 32-kDa xylanase was more effective in producing xylose and short xylooligomers. An assessment of the combined hydrolytic action of the two xylanases did not reveal any co-operative action. The sugars released when the two thermophilic xylanases were used together were almost identical to those released when the 32-kDa xylanase acted alone. The two xylanases were able to remove about 12% of the xylan remaining in an aspen kraft pulp. This indicated that either one of these thermophilic enzymes may be useful for enhancing the bleaching of kraft pulps. |
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Date de publication | 1993-12 |
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Dans | |
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Langue | anglais |
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Publications évaluées par des pairs | Oui |
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Numéro du CNRC | GILBERT1993 |
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Numéro NPARC | 9365471 |
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Exporter la notice | Exporter en format RIS |
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Signaler une correction | Signaler une correction (s'ouvre dans un nouvel onglet) |
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Identificateur de l’enregistrement | bd945bae-1100-4662-b1f4-688a986ebdd7 |
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Enregistrement créé | 2009-07-10 |
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Enregistrement modifié | 2020-04-24 |
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