Effect of high-intensity ultrasonic treatment on the emulsion of hemp seed oil stabilized with hemp seed protein

In this study, hemp seed oil (HSO) emulsions stabilized with hemp seed protein (HPI) were prepared and treated with high intensity ultrasonic (HIU). The effects of different treatment powers (0, 150, 300, 450, 600 W) on the properties, microstructure and stability of emulsions were investigated. HIU-treated emulsions showed improved emulsifying activity index and emulsifying stability index, reduced particle size, and increased absolute values of ζ-potential, with the extreme points of these indices occurring at a treatment power of 450 W. Here, the emulsion showed the best dispersion and the smallest particle size in fluorescence microscopy observation, with the highest adsorbed protein content (30.12%), and the highest tetrahydrocannabinol (THC) retention rate (87.64%). The best thermal and oxidative stability of the emulsions were obtained under HIU treatment with a power of 450 W. The D₄₃ and the peroxide values (POV) values after 30 d storage were the smallest at 985.74 ± 64.89 nm and 4.6 μmol/L, respectively. Therefore, 450 W was optimal HIU power to effectively improve the properties of HPI-stabilized HSO emulsion and promote the application of HSO and its derivatives in food processing production.     

基于CPCI总线DMA方式的实时高速数据交换系统

针对在重离子同步加速器运行过程中,如何解决设备控制器与上层数据处理程序之间的高速数据交换的问题,自主研发了基于Compact PCI总线板卡,板载FPGA,DSP,SDRAM等资源,并设计了DMA完整控制逻辑,传输协议解译全部由硬件完成（FPGA）。多个软硬件模块共同实现了该实时高速数据交换系统。该系统经实测,结构完整自洽,数据传输带宽符合重离子同步加速器运行要求,实现了数据传输的实时性。重点描述该系统数据通路上的诸多技术环节,包括硬件和软件的功能划分、FPGA、DSP、驱动程序、上层应用等各环节的技术细节。该实时数据交换系统系原创性设计,系统解决了控制与数据采集系统的设备控制层与上层数据处理层之间的实时数据交换问题。     

Stability of S-layer proteins for electrochemical nanofabrication

Crystalline cell surface layer proteins (S-layers) can be used in electrochemical fabrication to create nanoscale arrays of metals and oxides on surfaces so long as the proteins maintain their long-range order during processing. We have explored the stability of the HPI layer protein (the S-layer protein from the microorganism Deinococcus radiodurans) adsorbed onto platinum surfaces after immersion in sulfuric acid or sodium hydroxide electrolytes ranging in pH from 0 to 14 over time periods ranging from 1 to 1000 s. Topographic data obtained by atomic force microscopy (AFM) was used to characterize the protein stability, judged by its retention of long-range order after immersion. The compiled data revealed that, under these solution conditions and in this environment, the HPI layer protein has a dose-dependent structural stability “envelope” in the acidic range from 1 < pH < 4. The protein retains its long-range order up to 1000 s from pH 4 to 11, and has a sharp stability edge between pH 12 and 13. Interestingly, the more stringent requirement of stability (i.e., retention of long-range order) defined in the context of electrochemical fabrication for this protein narrowed the window of stability in pH and time when compared to previous stability studies reported for this protein.