Translucency mechanism of heat-induced pigeon egg white gel.

In this study, the properties of pigeon egg white (PEW) and chicken egg white (CEW) thermal gels were compared, with the aim of revealing the mechanisms involved in the high transparency of PEW thermal gels. Results demonstrated that PEW gels exhibited higher transparency than CEW gels. Scanning electron microscope (SEM) and transmission electron microscope (TEM) analysis revealed that PEW gels formed a fine chain gel network structure with an average diameter of thermal aggregates (89.84 ± 7.13 nm). The molecular properties of PEW proteins, such as higher content of ß-sheet structures (32.73 %), reactive groups (free sulfhydryl groups, hydrophobic groups), and absolute zeta potential (-3.563 mV), were found to contribute to the formation of smaller thermal aggregates during thermal denaturation. The microrheology measurements showed that these features allowed PEW proteins to interact less with each other and form smaller thermal aggregates during thermal denaturation, which facilitated the formation of fine chain gel networks and thus improved the transparency of the gels. The present study initially reveals the molecular basis of the high transparency of PEW thermal gels and provides a theoretical reference for the development of new highly transparent protein materials.

Copper-mediated oxidative C-H/N-H activations with alkynes by removable hydrazides.

The efficient copper-mediated oxidative C-H alkynylation of benzhydrazides was accomplished with terminal alkynes. Thus, a heteroaromatic removable N-2-pyridylhydrazide allowed for domino C-H/N-H functionalization. The approach featured remarkable functional group compatibility and ample substrate scope. Thereby, highly functionalized aromatic and heteroaromatic isoindolin-1-ones were accessed with high efficacy with rate-limiting C-H cleavage.