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Stabilization of iron-arsenic deposits by encapsulation with montmorillonite inorganic gels
Jingmin Yan,Yongliang Wang,Yanhua Wang,Xiang Liu,Shufeng Ye 대한환경공학회 2022 Environmental Engineering Research Vol.27 No.2
Encapsulation is recognized as an effective technique for enhancing the stability of hazardous waste by coating it with an inert material. In this work, an eco-friendly montmorillonite (Mt) inorganic gel with the characteristics of high viscosity, adsorption and easy preparation was developed and coated on the surface of iron-arsenic deposits (IAD) to restrain the release of arsenic (As). The encapsulation system investigated involves Mt/IAD mass ratio and aging temperature of the coated iron-arsenic deposits (C-IAD). The C-IAD was characterized by XRF, XRD, SEM-EDS, TEM, FTIR and BET. The results revealed that the IAD was completely encapsulated by the montmorillonite inorganic gel. From the experiment of stability, when IAD was coated with montmorillonite inorganic gel (Mt/IAD mass ratio 0.75) and aged at 25℃, As release decreased from 3.15 mg/L to 0.64 mg/L at pH 5 after 24 h, and then dropped to 0.11 mg/L after 7 d. Furthermore, the results indicated that the IAD encapsulated with montmorillonite inorganic gel was effective in suppressing the release of As under both weakly acidic and alkaline conditions.
Shuang Wang,Jingmin Gu,Meng Lv,Zhimin Guo,Guangmou Yan,Ling Yu,Chongtao Du,Xin Feng,Wenyu Han,Changjiang Sun,Liancheng Lei 한국미생물학회 2017 The journal of microbiology Vol.55 No.5
Bacteriophage endolysin is one of the most promising antibioticsubstitutes, but in Gram-negative bacteria, the outermembrane prevents the lysin from hydrolyzing peptidoglycansand blocks the development of lysin applications. Theprime strategy for new antibiotic substitutes is allowing lysinto access the peptidoglycan from outside of the bacteria byreformation of the lysin. In this study, the novel Escherichiacoli (E. coli) phage lyase lysep3, which lacks outside-in catalyticability, was fused with the N-terminal region of theBacillus amyloliquefaciens lysin including its cell wall bindingdomain D8 through the best manner of protein fusionbased on the predicted tertiary structure of lysep3-D8 to obtainan engineered lysin that can lyse bacteria from the outside. Our results showed that lysep3-D8 could lyse both Gramnegativeand Gram-positive bacteria, whereas lysep3 and D8have no impact on bacterial growth. The MIC of lysep3-D8on E. coli CVCC1418 is 60 μg/ml; lysep3-D8 can inhibit thegrowth of bacteria up to 12 h at this concentration. The bactericidalspectrum of lysep3-D8 is broad, as it can lyse of allof 14 E. coli strains, 3 P. aeruginosa strains, 1 Acinetobacterbaumannii strain, and 1 Streptococcus strain. Lysep3-D8 hassufficient bactericidal effects on the 14 E. coli strains testedat the concentration of 100 μg/ml. The cell wall binding domainof the engineered lysin can destroy the integrity of theouter membrane of bacteria, thus allowing the catalytic domainto reach its target, peptidoglycan, to lyse the bacteria. Lysep3-D8 can be used as a preservative in fodder to benefitthe health of animals. The method we used here proved to bea successful exploration of the reformation of phage lysin.