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Environmentally Friendly Flexible Strain Sensor from Waste Cotton Fabrics and Natural Rubber Latex.

ABSTRACT: A green approach was successfully developed to fabricate flexible sensors by utilizing carbonized waste cotton fabrics in combination with natural rubber latex. Waste cotton fabrics were firstly carbonized by heat treatment in the nitrogen atmosphere before they were combined with natural rubber latex using three methods, i.e., vacuum bagging, negative pressure adsorption and drop coating. After impregnation with natural rubber, the carbonized cotton maintained the fabric structure and showed good conductivity. More importantly, the electric resistance of the textile composites changed with the tensile strain. The cyclic stretching-releasing tests indicated that the prepared wearable flexible strain sensors were sensitive to strain and stable under cyclic loading. The flexible strain sensor also demonstrated the capability of monitoring human finger and arm motion.

SUBMITTER: Chen X

PROVIDER: S-EPMC6473477 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature

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Environmentally Friendly Flexible Strain Sensor from Waste Cotton Fabrics and Natural Rubber Latex.

Chen Xinzhu X An Jing J Cai Guangming G Zhang Jin J Chen Wu W Dong Xiongwei X Zhu Licheng L Tang Bin B Wang Jinfeng J Wang Xungai X

Polymers 20190301 3

A green approach was successfully developed to fabricate flexible sensors by utilizing carbonized waste cotton fabrics in combination with natural rubber latex. Waste cotton fabrics were firstly carbonized by heat treatment in the nitrogen atmosphere before they were combined with natural rubber latex using three methods, i.e., vacuum bagging, negative pressure adsorption and drop coating. After impregnation with natural rubber, the carbonized cotton maintained the fabric structure and showed go ...[more]

PMID: 30960388

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Project description:Gram-positive rubber degraders such as Streptomyces sp. strain K30 cleave rubber [poly(cis-1,4-isoprene)] to low-molecular-mass oligoisoprenoid products with terminal keto and aldehyde groups by the secretion of a latex clearing protein (Lcp) designated rubber oxygenase. LcpK30 is a heme b cytochrome and has a domain of unknown function (DUF2236) that is characteristic of orthologous Lcps. Proteins with a DUF2236 domain are characterized by three highly conserved residues (R164, T168, and H198 in LcpK30). Exchange of R164 or T168 by alanine and characterization of the purified LcpK30 muteins revealed that both were stable and contained a heme group (red color) but were inactive. This finding identifies both residues as key residues for the cleavage reaction. The purified H198A mutein was also inactive and stable but was colorless due to the absence of heme. We constructed and characterized alanine muteins of four additional histidine residues moderately conserved in 495 LcpK30 homologous sequences (H203A, H232A, H259A, H266A). All muteins revealed wild-type properties, excluding any importance for activity and/or heme coordination. Since LcpK30 has only eight histidines and the three remaining residues (H103, H184, and H296) were not conserved (<11%), H198 presumably is the only essential histidine, indicating its putative function as a heme ligand. The second axial position of the heme is likely occupied by a not yet identified molecule. Mutational analysis of three strictly conserved arginine residues (R195, R202, R328) showed that R195A and R202A muteins were colorless and instable, suggesting that these residues are important for the protein stability.ImportanceLarge amounts of rubber waste materials have been permanently released into the environment for more than a century, yet accumulation of rubber particles released, e.g., by abrasion of tires along highways has not been observed. This is indicative of the ubiquitous presence and activity of rubber-degrading microorganisms. Despite increasing research activities on rubber biodegradation during the last 2 decades, the knowledge of the enzymatic cleavage mechanism of rubber by latex clearing protein (Lcp) still is limited. In particular, the catalytic cleavage mechanism and the amino acids of Lcp proteins (Lcps) that are involved have not yet been identified for any Lcp. In this study, we investigated the importance of 10 amino acid residues of Lcp from Streptomyces sp. K30 (LcpK30) by mutagenesis, mutein purification, and biochemical characterization. We identified several essential residues, one of which most likely represents an axial heme ligand in Lcp of Streptomyces sp. K30.

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Dataset Information

Environmentally Friendly Flexible Strain Sensor from Waste Cotton Fabrics and Natural Rubber Latex.

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Environmentally Friendly Flexible Strain Sensor from Waste Cotton Fabrics and Natural Rubber Latex.

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