Harnessing Persistent Photocurrent in a 2D Semiconductor-Polymer Hybrid Structure: Electron Trapping and Fermi Level Modulation for Optoelectronic Memory.

Recently, 2D semiconductor-based optoelectronic memory has been explored to overcome the limitations of conventional von Neumann architectures by integrating optical sensing and data storage into one device. Persistent photocurrent (PPC), essential for optoelectronic memory, originates from charge carrier trapping according to the Shockley-Read-Hall (SRH) model in 2D semiconductors. The quasi-Fermi level position influences the activation of charge-trapping sites. However, the correlation between quasi-Fermi level modulations and PPC in 2D semiconductors has not been extensively studied. In this study, we demonstrate optoelectronic memory based on a 2D semiconductor-polymer hybrid structure and confirm that the underlying mechanism is charge trapping, as the SRH model explains. Under light illumination, electrons transfer from polyvinylpyrrolidone to p-type tungsten diselenide, resulting in high-level injection and majority carrier-type transitions. The quasi-Fermi level shifts upward with increasing temperature, improving PPC and enabling optoelectronic memory at 433 K. Our findings offer valuable insights into optimizing 2D semiconductor-based optoelectronic memory.

Depth map generation using a single image sensor with phase masks.

Conventional stereo matching systems generate a depth map using two or more digital imaging sensors. It is difficult to use the small camera system because of their high costs and bulky sizes. In order to solve this problem, this paper presents a stereo matching system using a single image sensor with phase masks for the phase difference auto-focusing. A novel pattern of phase mask array is proposed to simultaneously acquire two pairs of stereo images. Furthermore, a noise-invariant depth map is generated from the raw format sensor output. The proposed method consists of four steps to compute the depth map: (i) acquisition of stereo images using the proposed mask array, (ii) variational segmentation using merging criteria to simplify the input image, (iii) disparity map generation using the hierarchical block matching for disparity measurement, and (iv) image matting to fill holes to generate the dense depth map. The proposed system can be used in small digital cameras without additional lenses or sensors.

Radiographic and computed tomographic features of caval foramen hernias of the liver in 7 dogs: mimicking lung nodules.

This study describes the imaging features and characteristics of caval foramen hernias in 7 dogs diagnosed by computed tomography (CT). On lateral radiographs, 6 of 7 dogs showed dome-shaped, broad-based, caudal mediastinal lesions. CT findings included caudal vena cava (CVC) compression (n=7), right lateral (n=6) or medial (n=1) liver lobe involvement, hepatic vein dilation (n=5) and biliary tract involvement (n=1) with partial (n=6) or entire (n=1) liver lobe hernias. A caval foramen hernia should be part of the differential diagnosis when the aforementioned imaging features are detected. CT is considered as a useful tool for diagnosis and evaluation in dogs with a caval foramen hernia.

Development and evaluation of efficient recombinant Escherichia coli strains for the production of 3-hydroxypropionic acid from glycerol.

3-Hydroxypropionic acid (3-HP) is a commercially valuable chemical with the potential to be a key building block for deriving many industrially important chemicals. However, its biological production has not been well documented. Our previous study demonstrated the feasibility of producing 3-HP from glycerol using the recombinant Escherichia coli SH254 expressing glycerol dehydratase (DhaB) and aldehyde dehydrogenase (AldH), and reported that an "imbalance between the two enzymes" and the "instability of the first enzyme DhaB" were the major factors limiting 3-HP production. In this study, the efficiency of the recombinant strain(s) was improved by expressing DhaB and AldH in two compatible isopropyl-thio-beta-galactoside (IPTG) inducible plasmids along with glycerol dehydratase reactivase (GDR). The expression levels of the two proteins were measured. It was found that the changes in protein expression were associated with their enzymatic activity and balance. While cloning an alternate aldehyde dehydrogenase (ALDH), alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH), instead of AldH, the recombinant E. coli SH-BGK1 showed the highest level of 3-HP production (2.8 g/L) under shake-flask conditions. When an aerobic fed-batch process was carried out under bioreactor conditions at pH 7.0, the recombinant SH-BGK1 produced 38.7 g 3-HP/L with an average yield of 35%. This article reports the highest level of 3-HP production from glycerol thus far.

Cloning, expression, and characterization of an aldehyde dehydrogenase from Escherichia coli K-12 that utilizes 3-Hydroxypropionaldehyde as a substrate.

3-Hydroxypropionaldehyde (3-HPA), an intermediary compound of glycerol metabolism in bacteria, serves as a precursor to 3-Hydroxypropionic acid (3-HP), a commercially valuable platform chemical. To achieve the effective conversion of 3-HPA to 3-HP, an aldH gene encoding an aldehyde dehydrogenase in Escherichia coli K-12 (AldH) was cloned, expressed, and characterized for its properties. The recombinant AldH exhibited broad substrate specificity for various aliphatic and aromatic aldehydes. AldH preferred NAD+ over NADP+ as a cofactor for the oxidation of most aliphatic aldehydes tested. Among the aldehydes used, the specific activity was highest (38.1 U mg(-1) protein) for 3-HPA at pH 8.0 and 37 degrees C. The catalytic efficiency (kcat) and the specificity constant (kcat/Km) for 3-HPA in the presence of NAD+ were 28.5 s(-1) and 58.6x10(3) M(-1) s(-1), respectively. The AldH activity was enhanced in the presence of disulfide reductants such as dithiothreitol (DTT) or 2-mercaptoethanol, while several metal ions, particularly Hg2+, Ag+, Cu2+, and Zn2+, inhibited AldH activity. This study illustrates that AldH is a potentially useful enzyme in converting 3-HPA to 3-HP.