Assessing the effect of new control and payment methods on heating energy consumption and occupant behaviour in Chinese dwellings

Energy demand reduction has become a global issue involving all countries, including China. As major energy consumers in today s society, the need for buildings to be built and operated more energy efficiently is well recognized. In 1995, the national standard on building energy efficiency in China (JGJ 26-95) was refined and updated to become the new residential Buildings standard (JGJ 26-2010) published in 2010. In the new version, many changes have been made to support the construction of more energy efficient buildings in China. For example, in the new standard, all buildings are highly recommended to install personal control on the heating system, such as by Thermostatic Radiator Valves (TRVs), together with pay for what you use tariffs. Previous practice comprised uncontrolled heating with payment based on floor area. In order to reduce building energy consumption, Chinese government has revised the Chinese building design standard. In the new guide the use of individual room temperature control is highly recommended for new and refurbishment buildings. However, evidence to quantify the extent to which this improvement impact upon on the building energy consumption is currently lacking. This thesis evaluates the impact of updated building design standards on thermal conditions and energy consumption in Chinese residential buildings. In order to evaluate the impact on the building energy consumption, two types of residential buildings have been chosen, one complying with the old Chinese building design standard, while the other complies with the new standard. The study was carried out in seven apartments in each type of building, a total of fourteen apartments and comprised with a longitudinal monitoring of indoor air temperature, outdoor air temperature, window position and energy consumption of each apartment. The impact of the new design standard has been evaluated in relation to a number of aspects, that include building construction, indoor thermal environment, occupant behaviour, thermal comfort and building energy consumption. It is concluded that updating the building design standard has had a positive influence on the building conditions and energy consumption. Furthermore, a thermal comfort survey was carried out in both new and old apartments according to updated standards. The results show that the Predicted Mean Vote (PMV) model has a efficiently adequate predictor of occupants thermal comfort in both type of apartments. Thereby allowing confirmation that the new control refine did not compromise on thermal comfort. The percentage of acceptable of occupants is higher in new apartments compared with the old apartments

Identification of α-MMC and MAP30 as glycoprotein and pI analysis.

<p>(A) The identification of purified two proteins, α-MMC and MAP30, as glycoproteins by periodic acid-Schiff's staining on SDS-PAGE. Lane 1 and 2 presented the purified α-MMC and MAP30. (B) Determination of pI of these two proteins on IEF-Polyacrylamide gel electrophoresis. Lane1 and 2 presented the purified MAP30 and α-MMC, respectively. Lane M presented broad pI calibration kit with Amyloglucosidase 3.50, Soybean trypsin inhibitor 4.55, β-Lactoglobulin A 5.20, Carbonic anhydrase B bovine 5.85, Carbonic anhydrase B human 6.55, Myoglobin horse 7.35, Lentil lectin-acidic band 8.15, Lentil lectin-middle band 8.45, Lentil lectin-basic band 8.65, Trypsinogen 9.30.</p

Topological inactivation activities.

<p>Lane 1 indicated pUC18 as a control; Lane 2 indicated the products of pUC18 DNA treated with α-MMC; Lane M indicated DNA ladder; Lane 3 indicated the products of pUC18 DNA treated with MAP30.</p

Comparison of SOD activity in crude extract, α-MMC and MAP30.

<p><b>Note</b>: Each data represented the average of three independent experiments tested in quadruplicate.</p

Elution profile of α-MMC and MAP30 on gel filtration and SP column.

<p>(A) Chromatography of fraction from SP-Sepharose FF on Sephacryl S-100HR column. After concentration, sample was added to the Sephacryl S-100HR chromatography (2.5 cm×120 cm) and eluted with a pH 6.5 10 mM sodium phosphate buffer containing 0.15 M NaCl at flow rate of 2 ml/min. Peak I was collected fraction. (B) Chromatography of fraction from Sephacryl S-100 column on Macro-Cap-SP Column. After desalting out and exchanging buffer of fraction from Sephacryl S-100, chromatography was loaded to Macro-Cap-SP column and eluted with 10 mM NaCl in pH 6.0 50 mM sodium phosphate. Finally a linear gradient from 50 mM NaCl to 150 mM NaCl in the same buffer at flow rate of 2 ml/min was used as eluent. Two fractions were collected and identified as α-MMC and MAP30, respectively.</p

Analysis of extracts and eluents from different stages of purification by SDS–Polyacrylamide gel electrophoresis.

<p>Lane 1–6 was in the presence of 2-mercapoethanol. Lane 1 presented the crude extract after acidic treatment; Lane 2 presented the fractionation after 60% A.S. precipitation; Lane 3 presented the eluent from SP-Sepharose FF chromatography; Lane 4 presented the eluent from gel filtration chromatography; Lane 5 presented peak 1, 20 µg of α-MMC, from Macro-Cap-SP chromatography; Lane 6 presented peak 2, 20 µg of MAP30, from Macro-Cap-SP chromatography. Lane 7–8 was in the absence of 2-mercapoethanol. Lane 7 presented peak 1, 20 µg of α-MMC, from Macro-Cap-SP chromatography; Lane 8 presented peak 2, 20 µg of MAP30, from Macro-Cap-SP chromatography.</p

Purification of α-MMC and MAP30 from 400 g of bitter melon seeds.

<p><b>Note</b>: Data documented were the average value of 5 different preparations.</p

Size, homogeneity and subunit structure analysis of two purified proteins by electrophoresis and MALDI-TOF/TOF.

<p>(A) Homogeneity analysis of two purified proteins on acidic discontinuous native polyacrylamide gel electrophoresis on the basis of the charges of required proteins. Lane 1,2 presented 20 µg and 15 µg α-MMC; Lane 3,4,5 presented 20 µg,10 µg and 15 µg MAP30. (B) Analysis of the size, homogeneity and subunit structure of two proteins by SDS-PAGE in the presence and absence of 2-mercaptoethanol. Lane 1,2 indicated 10 µg and 20 µg α-MMC; Lane 3,4 indicated 10 µg and 20 µg MAP30; Lane 5 indicated LMW calibration kit (Phophorylase b 97 kDa, Albumin 66 kDa, Ovalbumin 45 kDa, Carbonic anhydrase 30 kDa, Trypsin inhibitor 20.1 kDa, α-Lactalbumin 14.4 kDa). (C) Molecular weight determination of α-MMC and MAP30. Left presented the analytic result for α-MMC on MALDI-TOF/TOF; Right presented the analytic result for MAP30 on MALDI-TOF/TOF.</p

Multiple Colors Output on Voile through 3D Colloidal Crystals with Robust Mechanical Properties

Distinguished from the chromatic mechanism of dyes and pigments, structural color is derived from physical interactions of visible light with structures that are periodic at the scale of the wavelength of light. Using colloidal crystals with coloring functions for fabrics has resulted in significant improvements compared with chemical colors because the structural color from colloidal crystals bears many unique and fascinating optical properties, such as vivid iridescence and nonphotobleaching. However, the poor mechanical performance of the structural color films cannot meet actual requirements because of the weak point contact of colloidal crystal particles. Herein, we demonstrate in this study the patterning on voile fabrics with high mechanical strength on account of the periodic array lock effect of polymers, and multiple structural color output was simultaneously achieved by a simple two-phase self-assembly method for printing voile fabrics with 3D colloidal crystals. The colored voile fabrics exhibit high color saturation, good mechanical stability, and multiple-color patterns printable. In addition, colloidal crystals are promising potential substitutes for organic dyes and pigments because colloidal crystals are environmentally friendly

Detection of the SOD activity of crude extract, α-MMC and MAP30 on acidic PAGE.

<p>Lane 1∼3 stained by NBT; Lane 4∼6 stained by Coomassie brilliant blue R-250; Lane 1,4 presented crude extract of bitter melon seeds(50 µg of protein). Lane 2,5 presented α-MMC (20 µg). Lane 3,6 presented MAP30(20 µg).</p