As an essential food ingredient with good nutritional and functional properties and health benefits, eggs are widely utilized in food formulations. In particular, egg proteins have good emulsification properties and can be commonly used in various food products, such as mayonnaise and baked goods. Egg protein particles can act as stabilizers for Pickering emulsions because they can effectively adsorb at the oil-water interface, reduce interfacial tension, and form a stable physical barrier. Due to their emulsifying properties, biocompatibility, controlled release capabilities, and ability to protect bioactive substances, egg proteins have become ideal carriers for encapsulating and delivering functional substances. The focus of this review is to summarize current advances in using egg proteins as emulsifiers. The effects of influencing factors (temperature, pH, and ionic strength) and various modification methods (physical, chemical, and biological modification) on the emulsifying properties of egg proteins are discussed. In addition, the application of egg proteins as emulsifiers in food products is presented. Through in-depth research on the emulsifying properties of egg proteins, the optimization of their applications in food, biomedical, and other fields can be achieved.
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http://dx.doi.org/10.1111/1541-4337.70004 | DOI Listing |
J Appl Microbiol
January 2025
ICAR-Indian Institute of Horticultural Research, Hessaraghatta Lake Post, Bengaluru 560089, India.
Aim: Bacillus subtilis is usually found in soil, and their biocontrol and plant growth promoting capabilities are being explored more recently than ever. However, knowledge about metabolite production and genome composition of endophytic Bacillus subtilis from seeds is limited. In the present study, Bacillus subtilis EVCu15 strain isolated from the seeds of Vasconcellea cundinamarcensis (mountain papaya) was subjected to whole genome sequencing, and detailed molecular and functional characterization.
View Article and Find Full Text PDFPLoS One
January 2025
Department of Entomology and Plant Pathology, North Carolina State University, Raleigh, North Carolina, United States of America.
Ruvbl1 (also known as TIP49, Pontin) encodes an ATPase of the AAA+ protein superfamily involved in several cellular functions, including chromatin remodeling, control of transcription, and cellular development (motility, growth, and proliferation). While its role has been well established in model organisms including vertebrates and invertebrates (e.g.
View Article and Find Full Text PDFSci Rep
January 2025
Center of Excellence in Vaccine Research and Development (Chula Vaccine Research Center-Chula VRC), Faculty of Medicine, Chulalongkorn University, Bangkok, 10330, Thailand.
Delivery of an mRNA formulated with lipid nanoparticles (LNPs) induces robust humoral and cell-mediated branches of the immune response. Depending on the LNP formula, mRNA encoding proteins can be detected in the liver upon intramuscular administration of mRNA/LNP in mice. This study investigated the impact of mRNA/LNP administration on liver-associated macrophages at the transcriptomic and epigenetic levels in a mouse model.
View Article and Find Full Text PDFBMC Genomics
January 2025
Animal Science College, Zhejiang University, Zijingang Campus, Hangzhou, Zhejiang, 310058, China.
Background: The Taihe black-boned silky fowl, a distinguished indigenous breed of chicken, is renowned for its dual utility in both traditional medicinal and culinary applications. However, the breed faces significant challenges due to its suboptimal reproductive capabilities and a notably brief egg-laying period, which have impeded its broader development and cultivation. In this research endeavor, we employed an advanced, rapid DIA (Data independent acquisition) quantitative proteomics method on the Astral platform to meticulously analyze the ovarian proteome of these chickens.
View Article and Find Full Text PDFJ Chem Inf Model
January 2025
Laboratório de Genômica Aplicada e Bioinovações - Instituto Oswaldo Cruz/Fiocruz, Rio de Janeiro, Brazil 21040-900.
Protein dynamics is essential for various biological processes, influencing functions such as enzyme activity, molecular recognition, and signal transduction. However, traditional protein engineering methods often focus on static structures, lacking tools to precisely manipulate dynamic behaviors. Here, we developed Mutational Energy Landscape Trap (MELT), a novel method designed to control protein dynamics by combining Normal Mode Analysis (NMA) and mutagenesis.
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