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A cocoon silk chemistry strategy to ultrathin N-doped carbon nanosheet with metal single-site catalysts.

ABSTRACT: Development of single-site catalysts supported by ultrathin two-dimensional (2D) porous matrix with ultrahigh surface area is highly desired but also challenging. Here we report a cocoon silk chemistry strategy to synthesize isolated metal single-site catalysts embedded in ultrathin 2D porous N-doped carbon nanosheets (M-ISA/CNS, M?=?Fe, Co, Ni). X-ray absorption fine structure analysis and spherical aberration correction electron microscopy demonstrate an atomic dispersion of metal atoms on N-doped carbon matrix. In particular, the Co-ISA/CNS exhibit ultrahigh specific surface area (2105?m²?g^-1) and high activity for C-H bond activation in the direct catalytic oxidation of benzene to phenol with hydrogen peroxide at room temperature, while the Co species in the form of phthalocyanine and metal nanoparticle show a negligible activity. Density functional theory calculations discover that the generated O?=?Co?=?O center intermediates on the single Co sites are responsible for the high activity of benzene oxidation to phenol.

SUBMITTER: Zhu Y

PROVIDER: S-EPMC6155020 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature

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A cocoon silk chemistry strategy to ultrathin N-doped carbon nanosheet with metal single-site catalysts.

Zhu Youqi Y Sun Wenming W Luo Jun J Chen Wenxing W Cao Tai T Zheng Lirong L Dong Juncai J Zhang Jian J Zhang Maolin M Han Yunhu Y Chen Chen C Peng Qing Q Wang Dingsheng D Li Yadong Y

Nature communications 20180921 1

Development of single-site catalysts supported by ultrathin two-dimensional (2D) porous matrix with ultrahigh surface area is highly desired but also challenging. Here we report a cocoon silk chemistry strategy to synthesize isolated metal single-site catalysts embedded in ultrathin 2D porous N-doped carbon nanosheets (M-ISA/CNS, M = Fe, Co, Ni). X-ray absorption fine structure analysis and spherical aberration correction electron microscopy demonstrate an atomic dispersion of metal atoms on N-d ...[more]

PMID: 30242151

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Project description:BackgroundCocoonase is a proteolytic enzyme that helps in dissolving the silk cocoon shell and exit of silk moth. Chemicals like anhydrous Na2CO3, Marseille soap, soda, ethylene diamine and tartaric acid-based degumming of silk cocoon shell have been in practice. During this process, solubility of sericin protein increased resulting in the release of sericin from the fibroin protein of the silk. However, this process diminishes natural color and softness of the silk. Cocoonase enzyme digests the sericin protein of silk at the anterior portion of the cocoon without disturbing the silk fibroin. However, no thorough characterization of cocoonase and sericin protein as well as imaging analysis of chemical- and enzyme-treated silk sheets has been carried out so far. Therefore, present study aimed for detailed characterization of cocoonase and sericin proteins, phylogenetic analysis, secondary and tertiary structure prediction, and computational validation as well as their interaction with other proteins. Further, identification of tasar silkworm (Antheraea mylitta) pupa stage for cocoonase collection, its purification and effect on silk sheet degumming, scanning electron microscope (SEM)-based comparison of chemical- and enzyme-treated cocoon sheets, and its optical coherence tomography (OCT)-based imaging analysis have been investigated. Various computational tools like Molecular Evolutionary Genetics Analysis (MEGA) X and Figtree, Iterative Threading Assembly Refinement (I-TASSER), self-optimized predicted method with alignment (SOPMA), PROCHECK, University of California, San Francisco (UCSF) Chimera, and Search Tool for the Retrieval of Interacting Genes/Proteins (STRING) were used for characterization of cocoonase and sericin proteins. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), protein purification using Sephadex G 25-column, degumming of cocoon sheet using cocoonase enzyme and chemical Na2CO3, and SEM and OCT analysis of degummed cocoon sheet were performed.ResultsPredicted normalized B-factors of cocoonase and sericin with respect to α and β regions showed that these regions are structurally more stable in cocoonase while less stable in sericin. Conserved domain analysis revealed that B. mori cocoonase contains a trypsin-like serine protease with active site range 45 to 180 query sequences while substrate binding site from 175 to 200 query sequences. SDS-PAGE analysis of cocoonase indicated its molecular weight of 25-26 kDa. Na2CO3 treatment showed more degumming effect (i.e., cocoon sheet weight loss) as compared to degumming with cocoonase. However, cocoonase-treated silk cocoon sheet holds the natural color of tasar silk, smoothness, and luster compared with the cocoon sheet treated with Na2CO3. SEM-based analysis showed the noticeable variation on the surface of silk fiber treated with cocoonase and Na2CO3. OCT analysis also exemplified the variations in the cross-sectional view of the cocoonase and Na2CO3-treated silk sheets.ConclusionsPresent study enlightens on the detailed characteristics of cocoonase and sericin proteins, comparative degumming activity, and image analysis of cocoonase enzyme and Na2CO3 chemical-treated silk sheets. Obtained findings illustrated about use of cocoonase enzyme in the degumming of silk cocoon at larger scale that will be a boon to the silk industry.

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A cocoon silk chemistry strategy to ultrathin N-doped carbon nanosheet with metal single-site catalysts.

Publications

A cocoon silk chemistry strategy to ultrathin N-doped carbon nanosheet with metal single-site catalysts.

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