Egg protein (EP) has a variety of functional properties, such as gelling, foaming, and emulsifying. The gel characteristics provide a foundation for applications in the food industry and research on EP. The proteins denature and aggregate to form a dense three‐dimensional gel network structure, with a process influenced by protein concentration, pH, ion type, and strength. In addition, the gelation properties of EP can be altered to varying degrees by applying different treatment conditions to EP. Currently, modification methods for proteins include physical modification (heat‐induced denaturation, freeze–thaw modification, high‐pressure modification, and ultrasonic modification), chemical modification (glycosylation modification, phosphorylation modification, acylation modification, ethanol modification, polyphenol modification), and biological modification (enzyme modification). Pidan, salted eggs, egg tofu, and other egg products have unique sensory properties, due to the gel properties of EP. In accessions, EP has also been used as a new ingredient in food packaging and biopharmaceuticals due to its gel properties. This review will further promote EP gel research and provide guidance for its full application in many fields.
Antibiotic-resistant pathogens are
a serious threat to global public
health. The emergence of drug-resistant pathogens is due to the improper
use of antibiotics, making the treatment of bacterial infections very
challenging. Here, we reported an efficient antibiotic delivery nanoparticle
to minimize antibiotic resistance. The nanoparticle was designed to
target the bacterial membrane using mesoporous silica nanoparticles
(MSNs) modified with an ovotransferrin-derived antimicrobial peptide
(OVTp12), enabling the antibiotic to be delivered to the vicinity
of the pathogenic bacteria. Moreover, we observed that OVTp12-modified
nanoparticles effectively inhibited the growth of Escherichia
coli
in vitro and in vivo. The nanoparticle with high biosafety could significantly downregulate
the expression of inflammation-related cytokines in infected tissues.
Thus, this novel bacterial targeted nanoparticle provides advantages
in minimizing bacterial drug resistance and treating bacterial infection.
Objectives:The aim of the study was to design and synthesise novel lactotransferrin-derived antimicrobial peptides (AMPs) with enhanced antibacterial activity against cariogenic bacteria. Methods: We obtained the LF-1 (WKLLRKAWKLLRKA) and LF-2 (GKLIWKLLRKAWKLLRKA) AMPs, based on the N-terminal functional sequence of lactotransferrin, and characterised their physicochemical properties and secondary structure. Their antibacterial activity against caries-associated bacteria was evaluated using bacterial susceptibility and time-killing assays, as well as transmission electron microscopy (TEM). The antibiofilm activity against Streptococcus mutans biofilms was determined using biofilm susceptibility assays and confocal laser scanning microscopy (CLSM). A rodent model of dental caries was adopted to evaluate their anticaries effectiveness in vivo. Results: Both peptides possessed an α-helical structure with excellent amphipathicity. LF-1 was effective against S. mutans and Actinomyces species, whereas LF-2 showed more potent antibacterial activity than LF-1 against a broader spectrum of tested strains. Both peptides inhibited the formation of S. mutans biofilm starting at 8 μmol/L and exerted effective eradication of S. mutans in preformed biofilms. Both peptides exhibited satisfactory biocompatibility and exerted significant anticaries effects in a rodent model. Conclusions: Both lactotransferrin-derived peptides displayed strong antimicrobial activity against cariogenic bacteria and S. mutans biofilm in vitro and effectively inhibited dental caries in vivo.
Enamel non-cavitated lesions (NCLs) are subsurface enamel porosity from carious demineralization. The developed enamel cannot repair itself once NCLs occurs. The regeneration of mineral crystals under biomimetic environment is an...
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