Xylanases of Cellulomonas flavigena: expression, biochemical characterization, and biotechnological potential

Four xylanases of Cellulomonas flavigena were cloned, expressed in Escherichia coli and purified. Three enzymes (CFXyl1, CFXyl2, and CFXyl4) were from the GH10 family, while CFXyl3 was from the GH11 family. The enzymes possessed moderate temperature stability and a neutral pH optimum. The enzymes we...

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Detalles Bibliográficos
Autores principales: Lisov, Alexander V., Belova, Oksana V., Lisova, Zoya A., Vinokurova, Nataliy G., Nagel, Alexey S., Andreeva-Kovalevskaya, Zhanna I., Budarina, Zhanna I., Nagornykh, Maxim O., Zakharova, Marina V., Shadrin, Andrey M., Solonin, Alexander S., Leontievsky, Alexey A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2017
Materias:
Original Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5209306/
https://www.ncbi.nlm.nih.gov/pubmed/28050845
http://dx.doi.org/10.1186/s13568-016-0308-7
Descripción
Sumario:Four xylanases of Cellulomonas flavigena were cloned, expressed in Escherichia coli and purified. Three enzymes (CFXyl1, CFXyl2, and CFXyl4) were from the GH10 family, while CFXyl3 was from the GH11 family. The enzymes possessed moderate temperature stability and a neutral pH optimum. The enzymes were more stable at alkaline pH values. CFXyl1 and CFXyl2 hydrolyzed xylan to form xylobiose, xylotriose, xylohexaose, xylopentaose, and xylose, which is typical for GH10. CFXyl3 (GH11) and CFXyl4 (GH10) formed the same xylooligosaccharides, but xylose was formed in small amounts. The xylanases made efficient saccharification of rye, wheat and oat, common components of animal feed, which indicates their high biotechnological potential.

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