Research Advances in Plant Protein-Based Products: Protein Sources, Processing Technology, and Food Applications.

Plant proteins are high-quality dietary components of food products. With the growing interest in sustainable and healthy food alternatives, plant proteins have gained significant attention as viable substitutes for animal-based proteins. Understanding the diversity of protein sources derived from plants, novel processing technology, and multiple applications is crucial for developing nutritious and sustainable plant protein-based products. This Review summarizes the natural sources of traditional and emerging plant proteins. The classifications, processing technologies, and applications of plant protein-based products in the food industry are explicitly elucidated. Moreover, the advantages and disadvantages of plant protein-based food products are revealed. Strategies such as protein fortification and complementation to overcome these shortcomings are critically discussed. We also demonstrate several issues that need to be addressed in future development.

Structure relationship of non-covalent interactions between lotus seedpod oligomeric procyanidins and glycated casein hydrolysate during digestion.

Procyanidin-amino acid interactions during transmembrane transport cause changes in the structural and physical properties of peptides, which limits further absorption of oligopeptide-advanced glycation end products (AGEs). In this study, glycated casein hydrolysates (GCSHs) were employed to investigate the structure and interaction mechanism of GCSH with lotus seedpod oligomeric procyanidin (LSOPC) complexes in an intestinal environment. LSOPC can interact with GCSH under certain conditions to form hydrogen bonds and hydrophobic interactions to form GCSH-LSOPC complexes. Results showed that procyanidin further leads to the transformation of a GCSH secondary structure and the increase of surface hydrophobicity (H0). The strongest non-covalent interaction between GCSH and (-)-epigallocatechin gallate (EGCG) was due to the polyhydroxy structure of EGCG. Binding site analysis showed that EGCG binds to the internal cavity of P1 to maintain the relative stability of the binding conformation. The antioxidant capacity of GCSH was remarkably elevated by GCSH-LSOPC. This study will provide a new reference for the accurate control of oligopeptide-AGEs absorption by LSOPC in vivo.

Discovery of the Relationship between Distribution and Aflatoxin Production Capacity of Aspergillusspecies and Soil Types in Peanut Planting Areas.

In order to study the relationship between the distribution and aflatoxin production capacity of Aspergillus species and soil types, 35 soil samples were collected from the main peanut planting areas in Xiangyang, which has 19.7 thousand square kilometers and is located in a special area with different soil types. The soil types of peanut planting areas in Xiangyang are mainly sandy loam and clay loam, and most of the soil is acidic, providing unique nature conditions for this study. The results showed that the Aspergillus sp. population in clay loam (9050 cfu/g) was significantly larger than that in sandy loam (3080 cfu/g). The percentage of atoxigenic Aspergillus strains isolated from sandy loam samples was higher than that from clay loam samples, reaching 58.5%. Meanwhile the proportion of high toxin-producing strains from clay loam (39.7%) was much higher than that from sandy loam (7.3%). Under suitable culture conditions, the average aflatoxin production capacity of Aspergillus isolates from clay loam samples (236.97 µg/L) was higher than that of strains from sandy loam samples (80.01 µg/L). The results inferred that under the same regional climate conditions, the density and aflatoxin production capacity of Aspergillus sp. in clay loam soil were significantly higher than that in sandy loam soil. Therefore, peanuts from these planting areas are at a relatively higher risk of contamination by Aspergillus sp. and aflatoxins.

Inhibitory effect of lotus seedpod oligomeric procyanidins on advanced glycation end product formation in a lactose-lysine model system

Background Industrial food processing induces protein glycation modifications and toxic advanced glycation end products (AGEs) which affect human health. Therefore, it is of interest to monitor AGEs in food processing. The present study was carried out to investigate the influence of lotus seedpod oligomeric procyanidin (LSOPC) concentrations, solution pH value and metal ions on AGE formation by heat treatment of lactose-lysine model solutions. Ne-(carboxymethyl) lysine (CML), as one of the common AGEs was also determined by HPLC-MS/MS in this experiment. Results The results showed that LSOPC can inhibit the formation of AGEs effectively at higher concentrations, lower temperature, and it can reverse the promotion function of metal ions because of its high inhibition activity. Also, LSOPC can inhibit CML formation in the Maillard reaction as well. Conclusion These results indicated that LSOPC could be used as functional food ingredients to inhibit AGE formation.