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Detailed structure information a highly thermostable Tb-cluster that based on a prodrug ligand of 2,4,5-trifluoro-3-methoxybenzoic acid.

ABSTRACT: In this brief data article, we present the precise structural information, PARD data and thermographic analysis of the Tb-cluster. Detailed structure, luminescence and detecting properties were discussed in our previous study (Zhao et al., 2017) [1]. The data includes the coordination modes of ligand, PXRD patterns of these Ln-MOFs, thermostability, detailed bond lengths and bond angles of the Tb-cluster.

SUBMITTER: Zeng C

PROVIDER: S-EPMC6143725 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature

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Detailed structure information a highly thermostable Tb-cluster that based on a prodrug ligand of 2,4,5-trifluoro-3-methoxybenzoic acid.

Zeng Chenghui C Zheng Kai K Wang Xue-Zheng XZ Li Hao-Ran HR Zhao Zhi-Peng ZP Zhong Shengliang S

Data in brief 20180830

In this brief data article, we present the precise structural information, PARD data and thermographic analysis of the Tb-cluster. Detailed structure, luminescence and detecting properties were discussed in our previous study (Zhao et al., 2017) [1]. The data includes the coordination modes of ligand, PXRD patterns of these Ln-MOFs, thermostability, detailed bond lengths and bond angles of the Tb-cluster. ...[more]

PMID: 30238034

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Project description:BACKGROUND: Complete enzymatic hydrolysis of xylan to xylose requires the action of endoxylanase and ?-xylosidase. ?-xylosidases play an important part in hydrolyzing xylo-oligosaccharides to xylose. Thermostable ?-xylosidases have been a focus of attention as industrially important enzymes due to their long shelf life and role in the relief of end-product inhibition of xylanases caused by xylo-oligosaccharides. Therefore, a highly thermostable ?-xylosidase with high specific activity has significant potential in lignocellulose bioconversion. RESULTS: A gene encoding a highly thermostable GH39 ?-xylosidase was cloned from Geobacillus sp. strain WSUCF1 and expressed in Escherichia coli. Recombinant ?-xylosidase was active over a wide range of temperatures and pH with optimum temperature of 70 °C and pH 6.5. It exhibited very high thermostability, retaining 50% activity at 70 °C after 9 days. WSUCF1 ?-xylosidase is more thermostable than ?-xylosidases reported from other thermophiles (growth temperature ? 70 °C). Specific activity was 133 U/mg when incubated with p-nitrophenyl xylopyranoside, with Km and Vmax values of 2.38 mM and 147 U/mg, respectively. SDS-PAGE analysis indicated that the recombinant enzyme had a mass of 58 kDa, but omitting heating prior to electrophoresis increased the apparent mass to 230 kDa, suggesting the enzyme exists as a tetramer. Enzyme exhibited high tolerance to xylose, retained approximately 70% of relative activity at 210 mM xylose concentration. Thin layer chromatography showed that the enzyme had potential to convert xylo-oligomers (xylobiose, triose, tetraose, and pentaose) into fermentable xylose. WSUCF1 ?-xylosidase along with WSUCF1 endo-xylanase synergistically converted the xylan into fermentable xylose with more than 90% conversion. CONCLUSIONS: Properties of the WSUCF1 ?-xylosidase i.e. high tolerance to elevated temperatures, high specific activity, conversion of xylo-oligomers to xylose, and resistance to inhibition from xylose, make this enzyme potentially suitable for various biotechnological applications.

Dataset Information

Detailed structure information a highly thermostable Tb-cluster that based on a prodrug ligand of 2,4,5-trifluoro-3-methoxybenzoic acid.

Publications

Detailed structure information a highly thermostable Tb-cluster that based on a prodrug ligand of 2,4,5-trifluoro-3-methoxybenzoic acid.

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