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Thermostatically controlled loads (TCLs) have great potential to participate in demand response (DR) programs due to their thermal storage and transfer characteristics. In this paper, we propose a grouping control strategy based on customer comfort and power matching degree for aggregated TCLs. We also model an individual TCL based on equivalent thermal parameter (ETP). The aggregated TCLs are modeled with the time-varying Markov chain and 2D state-bin transition with the consideration of their heterogeneities. A load selecting process is introduced based on a multi-scale priority sorting composed of normalized temperature distance, power rating similarity and controlled times. These indexes increase the accuracy and speed of the tracking response to the optimum control signal. The simulation results verify that the proposed control strategy has a comprehensive performance on the tracking response, customer comfort, and the fairness of TCLs participated in DR programs.

Traps baited with female-produced sex pheromones have been very effective in the monitoring and management of mirid bugs in numerous field trials. However, none of the target odorant receptors for sex pheromone components in Apolygus lucorum have been identified. Here, we identified one candidate sex pheromone receptor, AlucOR4, from A. lucorum. Quantitative real-time PCR (qPCR) analysis revealed that AlucOR4 was antennae-enriched and male-biased in adult A. lucorum. Xenopus oocyte expression system assays demonstrated that AlucOR4/AlucOrco was sensitive to two major sex pheromone constituents and exhibited high sensitivity to (E)-2-hexenyl butyrate (E2HB) and lower sensitivity to hexyl butyrate (HB). The expression level of target mRNA was significantly reduced (>80%) in dsAlucOR4-injected bugs after five days. The electroantennogram (EAG) responses of male antennae to E2HB and HB were also reduced significantly (~40%). Our findings suggest that AlucOR4 is essential to sex pheromone perception in A. lucorum.

In this paper, pinning combining with impulsive control scheme is adopted to investigate the synchronization of complex-variable dynamical network. Based on the Lyapunov function method and mathematical analysis technique, sufficient conditions for achieving synchronization is first analytically derived. This result extends the condition derived for real-variable dynamical network to complex-variable network. Further, adaptive strategy is adopted to relax the restrictions on the impulsive intervals and reduce the control cost. Noticeably, the proposed adaptive pinning impulsive control scheme is universal for different dynamical networks to some extent. The impulsive instants are chosen by solving a series of maximum problems subject to the derived conditions. Several numerical simulations are performed to illustrate the effectiveness and correctness of the derived theoretical results.

Traditional biological treatment for triphenylmethane dye effluent is stuck with the inaccessibility of dye molecules to intracellular dye-degrading enzyme, thus a high-efficiency and low-cost method for dye decolorization is highly desirable. Here we established a bioremediation approach to display triphenylmethane reductase (TMR) on the surface of Escherichia coli (E. coli) using N-terminal of ice nucleation protein as anchoring motif for triphenylmethane dye decolorization for the first time. Approximately 85% of recombinant protein positioning on the surface of E. coil cells exhibited high activity and stability. The optimal temperature and pH of the surface-displayed TMR are 50 °C and 8.5, respectively. Comparing with other reported microorganisms, the decolorization rate for malachite green of this engineered strain is the highest so far, reaching 640 μmol min(-1) g(-1) dry weight cells. These results indicate that this engineered E. coli strain is a very promising candidate for synthetic dye removal.

The main objective of this work was to investigate the biosorption performance of unmodified and Cetylpyridinium chloride (CPC)-modified biomass of Penicillium YW 01 for Acid Blue 25 (AB 25). Maximum biosorption capacity of AB 25 onto CPC-modified biosorbent was 118.48 mg g −1 under phosphoric–phosphate buffer with initial dye concentration of 200 mg L −1 at 30 °C. The biosorption pattern of AB 25 onto unmodified biosorbent in aqueous solution and phosphoric–phosphate buffer was well fitted with both Langmuir and Freundlich isotherm models. While the equilibrium data of CPC-modified biosorbent in aqueous solution and phosphoric–phosphate buffer failed to fit the Freundlich isotherm model, indicating the monolayer biosorption formed onto CPC-modified biosorbent. The values of initial biosorption rate of biosorbent in phosphoric–phosphate buffer were found to be higher than that of corresponding values in aqueous solution, indicating phosphoric–phosphate buffer enhanced the initial biosorption rate of biosorption process. Weber–Morris model analysis indicated that the boundary layer effect had more influence on the biosorption process in phosphoric–phosphate buffer. The BET surface area of CPC-modified biosorbent (0.5761 m 2 g −1 ) was larger than that of unmodified biomass (0.3081 m 2 g −1 ). Possible dye–biosorbent interactions were confirmed by Fourier transform infrared spectroscopy.

The gene gdh encoding an organic solvent-tolerant and alkaline-resistant NAD(P)-dependent glucose 1-dehydrogenase (LsGDH) was cloned from Lysinibacillus sphaericus G10 and expressed in Escherichia coli. The recombinant LsGDH exhibited maximum activity at pH 9.5 and 50 °C. LsGDH displayed high stability at a wide pH ranging from 6.5 to 10.0 and was stable after incubation at 30 °C for 1 week in 25 mM sodium phosphate buffer (pH 6.5) in the absence or presence of NaCl. The activity of LsGDH was enhanced by Li+, Na+, K+, NH4+, Mg2+, and EDTA at pH 8.0. LsGDH exhibited high tolerance to 60% DMSO, 30% acetone, 30% methanol, 30% ethanol, 10% n-propanol, 30% isopropanol, 60% n-hexanol and 30% n-hexane. The relationship between stability and chain length of the alcohols fit a Gaussian distribution model (R2≥0.94), and demonstrated lowest enzyme stability in C4-alcohol. The results suggested that LsGDH was potentially useful for coenzyme regeneration in organic solvents or under alkaline conditions.