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Chen Xulong,Shi Yunxi,Cai Yi-xi,Xie Junfeng,Yang Yinqin,Hou Daolong,Fan Yongsheng 한국탄소학회 2024 Carbon Letters Vol.34 No.3
For the regeneration of diesel particulate filters (DPF) using non-thermal plasma (NTP), both cost-effectiveness and regeneration efficiency should be raised. This study compared and contrasted the physicochemical characteristics of carbon black and engine particulate matter (PM). After carbon black was put into the DPF, an experimental setup for the oxidation of PM using NTP was created. The findings showed that carbon black and PM samples had comparable oxidation traits, micro-nanostructures, and C/O elemental ratios. O3, the main active species in NTP, was susceptible to heat breakdown, and the rate of decomposition of O3 increases with increasing temperature. The removal effectiveness of carbon black first improved and subsequently declined with an increase in the NTP injection flow rate during offline DPF regeneration using NTP at room temperature. A relatively high carbon black removal efficiency of 85.1% was achieved at an NTP injection flow rate of 30 L/min.
Yin Qin,Batbatan Christopher G.,Li Yongxing,Zhang Yonghui,Yang Qiuming,Xiao Anfeng 한국미생물·생명공학회 2024 Journal of microbiology and biotechnology Vol.34 No.1
In this study, carrageenase immobilization was evaluated with a concise and efficient strategy. Pomelo peel cellulose (PPC) modified by polyethyleneimine (PEI) using the physical absorption method was used as a carrier to immobilize carrageenase and achieved repeated batch catalysis. In addition, various immobilization and reaction parameters were scrutinized to enhance the immobilization efficiency. Under the optimized conditions, the enzyme activity recovery rate was more than 50% and 4.1 times higher than immobilization with non-modified pomelo peels. The optimum temperature and pH of carrageenase after immobilization by PEI-modified pomelo peel, at 60°C and 7.5 respectively, were in line with the free enzyme. The temperature resistance was reduced, inconsistent with free enzyme, and pH resistance was increased. A significant loss of activity (46.8%) was observed after reusing it thrice under optimal reaction conditions. In terms of stability, the immobilized enzyme conserved 76.0% of the initial enzyme activity after 98 days of storage. Furthermore, a modest decrease in the kinetic constant (Km) value was observed, indicating the improved substrate affinity of the immobilized enzyme. Therefore, modified pomelo peel is a verified and promising enzyme immobilization system for the synthesis of inorganic solvents.