Measuring the disparity among scientific disciplines using Library of Congress Subject Headings

Scientometrics - Examining the relationships among scientific disciplines is important today, but existing methods are limited by the contents and structure of their bibliographic databases. We...     

Ferulic acid and EGCG alter the structural characteristics of ovalbumin and its application in mineral loading

This study aims to fabricate mineral-loading nanocarriers using natural materials. The interaction patterns between ovalbumin (OVA) and four water-soluble polyphenols, namely ferulic acid (FA), (-)-Epigallo-catechin 3-gallate (EGCG), gallic acid (GA) and epicatechin (EC), were investigated. Results showed that the optimised conditions for preparing stable OVA–polyphenol complexes are at the OVA–polyphenol ratio of 4:1 at pH 6, under which OVA–FA and OVA–EGCG showed the highest stability and mineral-loading capacity among four OVA–polyphenol complexes. The fluorescence results indicated that the addition of EGCG and FA induced a significant fluorescence quenching to OVA. The interaction between OVA and polyphenols involved hydrogen bonding, hydrophobic interaction and electrostatic interaction. Fourier transform infrared spectroscopy (FTIR) analysis suggested that both FA and EGCG enhanced the stability and orderliness of the structure of OVA. The transmission electron microscopy images also exhibited the spherical structure of OVA after the addition of FA and EGCG. Furthermore, scanning electron microscope–energy dispersive X-ray spectrum results suggested that OVA–FA and OVA–EGCG complexes were better mineral carriers than OVA–GA and OVA–EC. This study may serve as the theoretical support for the promising application of OVA in the fabrication of mineral-loading nanocarriers in functional food and pharmaceutic.     

Effect of microwave heating time on the gel properties of chicken myofibrillar proteins and their formation mechanism

The present work was conducted to illustrate the mechanism of gel formation of myofibrillar proteins (MPs) under different microwave heating times. The results showed that the denaturation enthalpy (ΔH) of the MPs significantly decreased when the heating time increased from 3 to 9 s and then completely disappeared as the heating time progressed, indicating that the MPs gradually denatured and subsequently aggregated with increasing heating time, which was further verified by the changes in the secondary structure, electrophoretic bands, and gel properties (e.g., water holding capacity and textural profiles) of the MPs. Microstructural images indicated that the MP gel formed under 12 s had the most compact network, indicating that extended microwave heating time could induce quality deterioration of MP gels. Moreover, the hydrophobic forces, electrostatic forces, and disulphide bonds of the MPs gradually intensified with increasing microwave heating time, suggesting that both non-covalent and covalent bonds could promote molecular denaturation and subsequent aggregation of MPs. In addition, correlation analysis revealed that the changes in the molecular conformation of MPs induced by different microwave heating times could effectively regulate the formation of MP gels and their related properties.