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PVDF membrane with tea powder adhered for efficient separation of emulsified oil
Zhang Junshuang,Wu Yue,Xia Mengsheng,Yang Qijiang,Xu Qinyao,Feng Wenwen 한국화학공학회 2023 Korean Journal of Chemical Engineering Vol.40 No.10
Conventional oily wastewater treatment can remove slick oil and dispersed oil well, but it is difficult for it to remove emulsified oil. Nonetheless, the development of super wetting materials provides a key role in treating the emulsified oil, but there are some problems, such as expensive raw materials, complicated processes, as well as secondary pollution. In order to treat these problems, a brand-new oil/water separation membrane (TEA/PVDF membrane) was developed by combining the viscosity of sodium alginate (SA) and the filter tea powder (TEA) onto the surface of the polyvinylidene fluoride (PVDF) membrane by a vacuum pump. Furthermore, the underwater oleophobic angle reached 135o. Moreover, the oil-water separation experiments of oil-in-water emulsion utilizing TEA/PVDF membrane demonstrated excellent separation efficiency (99.6%) and good flux (254 L m−2 h−1 bar−1). Notably, upon ten cycles, the oil removal rate was still as high as 99.2%. Moreover, the TEA/PVDF membrane was able to separate oil-in-water emulsions in environments with strong acids, strong bases, and high salt concentrations, with a separation efficiency of over 95.9%. Such a novel oil/water separation membrane is economic, environmentally protective, and simple production process, which exhibits overwhelming potential in practical life for treating oily wastewater.
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( Qin Yao ),( Zhi Gang Hu ),( Jia Ping Xu ),( Ke Ping Chen ) 한국잠사학회 2005 International Journal of Industrial Entomology Vol.10 No.2
Ribosome-associated membrane protein 4 (RAMP4) is a membrane protein that exposes its N-terminal hydrophilic portion on the cytoplasmic side and spans the membrane close to the C-terminal end. RAMP4 has previously been reported to belong to the set of proteins that remains associated with membrane-bound ribosomes, and controls the glycosylation of major histocompatbility complex class II-associated invariant chain. RAMP4 also may be relative to the stabilization of membrane proteins in response to stress, with other components of translocon, and molecular chaperons in ER. Application of 5`-RACE technique with specially designed primer, we cloned a 715 bp cDNA fragment which contains a 195 bp ORF, termed RAMP4. The deduced protein has 64 amino acid residues and contains a putative transmembrane-spanning domain at the COOH terminus.
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