Response time characteristics of a transmissive uniformly doped GaAsP photocathode.

In this paper, the matrix difference method is used to calculate the photoelectron continuity equation and the outgoing electron flux density equation. The effects of the GaAsP/AlGaAsP recombination rate, electron diffusion coefficient, and activation layer thickness on the time-resolved characteristics and quantum efficiency of a GaAsP photocathode are systematically studied, and the accuracy of the theoretical calculation is verified by experiments. The response speed and quantum efficiency of the GaAsP photocathode can be greatly improved by adjusting the thickness of the GaAsP activation layer reasonably.

Enhanced P-Type GaN Conductivity by Mg Delta Doped AlGaN/GaN Superlattice Structure.

A method of combining the AlGaN/GaN superlattices and Mg delta doping was proposed to achieve a high conductivity p-type GaN layer. The experimental results provided the evidence that the novel doping technique achieves superior p-conductivity. The Hall-effect measurement indicated that the hole concentration was increased by 2.06 times while the sheet resistivity was reduced by 48%. The fabricated green-yellow light-emitting diodes using the achieved high conductivity p-type GaN layer showed an 8- and 10-times enhancement of light output power and external quantum efficiency, respectively. The subsequent numerical calculation was conducted by using an Advanced Physical Model of Semiconductor Device to reveal the mechanism of enhanced device performance. This new doping technique offers an attractive solution to the p-type doping problems in wide-bandgap GaN or AlGaN materials.

Production of ACE inhibitory peptides from sweet sorghum grain protein using alcalase: Hydrolysis kinetic, purification and molecular docking study.

In this study, sweet sorghum grain protein (SSGP) was hydrolyzed using alcalase yielding ACE inhibitory peptides. A kinetic model was proposed to describe the enzymolysis process of SSGP. The kinetic parameters, a and b, were determined according to experimental data. It was found that the model was reliable to describe the kinetic behaviour for SSGP hydrolysis by alcalase. After hydrolysis, the SSGP hydrolysate with DH of 19% exhibited the strongest ACE inhibitory activity and the hydrolysate was then used to isolate ACE inhibitory peptides. A novel ACE inhibitory peptide was successfully purified from this hydrolysate by ultrafiltration, ion exchange chromatography, gel filtration chromatography, and reversed-phased high performance liquid chromatography (RP-HPLC). The amino acid sequence of the purified peptide was identified as Thr-Leu-Ser (IC50=102.1 µM). The molecular docking studies revealed that the ACE inhibition of the tripeptide was mainly attributed to its C-terminal Ser, which can effectively interact with the S1 and S2 pockets of ACE. Our studies suggest that the tripeptide from the SSGP hydrolysate can be utilized to develop functional food ingredients or pharmaceuticals for prevention of hypertension.

A novel angiotensin-І converting enzyme (ACE) inhibitory peptide from gastrointestinal protease hydrolysate of silkworm pupa (Bombyx mori) protein: Biochemical characterization and molecular docking study.

Silkworm pupa (Bombyx mori) protein was hydrolyzed using gastrointestinal endopeptidases (pepsin, trypsin and α-chymotrypsin). Then, the hydrolysate was purified sequentially by ultrafiltration, gel filtration chromatography and RP-HPLC. A novel ACE inhibitory peptide, Ala-Ser-Leu, with the IC50 value of 102.15µM, was identified by IT-MS/MS. This is the first report of Ala-Ser-Leu from natural protein. Lineweaver-Burk plots suggest that the peptide is a competitive inhibitor against ACE. The molecular docking studies revealed that the ACE inhibition of Ala-Ser-Leu is mainly attributed to forming very strong hydrogen bonds with the S1 pocket (Ala354) and the S2 pocket (Gln281 and His353). The results indicate that silkworm pupa (B. mori) protein or its gastrointestinal protease hydrolysate could be used as a functional ingredient in auxiliary therapeutic foods against hypertension.