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

ABSTRACT: 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.

SUBMITTER: Lisov AV

PROVIDER: S-EPMC5209306 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature

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

Lisov Alexander V AV Belova Oksana V OV Lisova Zoya A ZA Vinokurova Nataliy G NG Nagel Alexey S AS Andreeva-Kovalevskaya Zhanna I ZI Budarina Zhanna I ZI Nagornykh Maxim O MO Zakharova Marina V MV Shadrin Andrey M AM Solonin Alexander S AS Leontievsky Alexey A AA

AMB Express 20170103 1

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 ...[more]

PMID: 28050845

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