Henan University of Technology

About: Henan University of Technology is a education organization based out in Zhengzhou, China. It is known for research contribution in the topics: Catalysis & Starch. The organization has 7648 authors who have published 6503 publications receiving 73067 citations. The organization is also known as: Hénán Gōngyè Dàxué.

Effect of Vacuum Impregnation Combined with Calcium Lactate on the Firmness and Polysaccharide Morphology of Kyoho Grapes ( Vitis vinifera x V. labrusca )

Abstract: The effects of vacuum impregnation (VI) with 2% calcium lactate treatment on the VI properties (obtained from hydrodynamic mechanism and deformation–relaxation phenomena models), firmness, and pectin of Kyoho grapes were investigated. Fruit pectin was analysed by atomic force microscopy (AFM). VI was applied for 10–35 min at 25–45 °C and 5 kPa. The maximum values of effective porosity, ee (0.606%), and volume fraction, X (0.588%), occurred at 35 °C when the VI time was 15 min. No change was observed in the volumetric deformation (γ ≈ 0) of the grapes after the impregnation. The firmness significantly increased at 35 °C VI (from 12.93 to 14.47 N). According to the AFM results, calcium mainly inhibited the degradation of chelate-soluble pectin and sodium carbonate-soluble pectin short branches during the VI. Under the studied conditions, the validity of VI to incorporate calcium into fruit to improve the quality of grapes was verified, and a final corresponding product was obtained by VI.

Spectroscopy and molecular docking study on the interaction behavior between nobiletin and pepsin.

Abstract: In this study, the binding mode of nobiletin (NOB) with pepsin was investigated by spectroscopic and molecular docking methods. NOB can interact with pepsin to form a NOB-pepsin complex. The binding constant, number of binding sites and thermodynamic parameters were measured, which indicated that NOB could spontaneously bind with pepsin through hydrophobic and electrostatic forces with one binding site. Molecular docking results revealed that NOB bound into the pepsin cavity. Synchronous and three-dimensional fluorescence spectra results provide data concerning conformational and some micro-environmental changes of pepsin. Furthermore, the binding of NOB can inhibit pepsin activity in vitro. The present study provides direct evidence at a molecular level to show that NOB could induce changes in the enzyme pepsin structure and function.