Adzuki beans are grown in several countries around the world and are widely popular in Asia, where they are often prepared in various food forms. Adzuki beans are rich in starch, and their proteins contain a balanced variety of amino acids with high lysine content, making up for the lack of protein content of cereals in the daily diet. Therefore, the research on adzuki beans and the development of their products have broad prospects for development. The starch, protein, fat, polysaccharide, and polyphenol contents and compositions of adzuki beans vary greatly among different varieties. The processing characteristic components of adzuki beans, such as starch, isolated protein, and heated flavor, are reported with a view to further promote the processing and development of adzuki bean foods. In addition to favorable edibility, the human health benefits of adzuki beans include antioxidant, antibacterial, and anti-inflammatory properties. Furtherly, adzuki beans and extracts have positive effects on the prevention and treatment of diseases, including diabetes, diabetes-induced kidney disease or kidney damage, obesity, and high-fat-induced cognitive decline. This also makes a case for the dual use of adzuki beans for food and medicine and contributes to the promotion of adzuki beans as a healthy, edible legume.

Perilla (Perilla frutescens) seeds are emerging as a valuable resource for functional foods and medicines owing to their rich oil and protein content with diverse nutritional and health benefits. Perilla seed oil (PSO) possesses a high level of a-linolenic acid (ALA), a favorable ratio of unsaturated to saturated fatty acids, and other active ingredients such as tocopherols and phytosterols, which contribute to its antioxidant, anti-inflammatory, and cardiovascular protective effects. The balanced amino acid ratio and good functional properties of perilla seed protein make it suitable for a variety of food applications. The chemical composition, health benefits, and potential applications of PSO as well as the structural characterization, functional properties, modification methods, bioactivities, and application scenarios of perilla seed protein are comprehensively presented in this paper. Furthermore, the challenges as well as future prospects and research focus of PSO and perilla seed protein are discussed. The growing interest in plant-based diets and functional foods has made PSO and perilla seed protein promising ingredients for the development of novel foods and health products. The purpose of this paper is to highlight implications for future research and development utilizing these two untapped resources to improve human health and nutrition.

In this paper, cellulose nanofibers (CNF) were prepared from wheat bran (WB) and the structure of CNF was determined. Fourier transform infrared spectra and X-ray diffractograms showed the groups such as hydroxyl and carboxyl groups and cellulose type 1 structure possessed by CNF, respectively. Scanning electron microscopy exhibited that CNF was filamentous and intertwined. In addition, Pickering emulsions were prepared using CNF and the physicochemical properties of the emulsions were characterized. The results showed that CNF was able to increase the zeta potential and viscosity of the emulsions, thus improving the stability of the emulsions. Moreover, CNF formed a physical barrier by adsorbing at the oil-water interface and near the oil droplets and CNF dispersed in the aqueous phase formed a network structure to restrict the movement of oil droplets, thus improving the stability of the emulsions. These findings may provide some new insights for the potential applications of WB.

To explore better methods of natural protein modification for black soybean, comparisons among the effects of different modified methods on structural changes of the modified products of black soybean protein isolate (BSPI) were carried out in this study. The modified products used in this study included enzymatic crossing-link black soybean protein isolate (ECBSPI), wet heating treatment glycosylation black soybean protein isolate (WHTGBSPI) and especially enzymatic glycosylation black soybean protein isolate catalyzed by transglutaminase (EGBSPI). The effects of the modification methods on structural changes were analyzed by SDS-polyacrylamide gel electrophoresis (SDS-PAGE), amino acid content and circular dichroism (CD) analysis. Moreover, the processing properties changes caused by structural changes of BSPI were detected by thermogravimetric analysis, particle size analysis, zeta-potential, surface hydrophobicity, solubility, emulsification, gelation, and rheological properties. The results show that the modified BSPI products were protein polymers, and among them, EGBSP and WHTGBSPI are covalently bonded glycation products. Products modified by Maillard reactions and transglutaminase (TG) display partly destroyed α-helix and β-sheet structures that form more open secondary BSPI structures. For ECBSPI, the proportion of irregular crimp structure reduces to form a high order secondary structure. All the modified products form fine aggregations in dispersion, except WHTGBSPI has most negative zeta-potential and least molecular stability due to the hydrophobic amino acids embedded in the protein molecules. The zeta-potentials of BSPI, ECBSPI, WHTGBSPI and EGBSPI are respectively −21.5, −23.8, −18.1 and −20.2 mV. The surface hydrophobicity of EGBSPI (5.07 ± 0.07) and WHTGBSPI (7.02 ± 0.05) decrease, while the surface hydrophobicity of ECBSPI (19.5 ± 0.06) increases. The solubility and rheological properties of EGBSPI, ECBSPI and WHTGBSPI after modification are all better than those of BSPI, especially EGBSPI. Emulsification of EGBSPI and WHTGBSPI increase (by 24.5% and 12.2%, respectively) while ECBSPI decrease (by 17.0), and there is similar emulsion stability trend. Moreover, the properties of ECBSPI increase except cohesiveness compared to BSPI. In conclusion, as a safe and efficient method for natural protein modification, enzymatic glycosylation catalyzed by TG has great potential in improving food processing characteristics.

The study aimed to investigate the effect of germination conditions on the content of polyphenol extract in mung bean and to further investigate the effect of polyphenol extract in germinated mung bean on diabetic mice. Through single factor experiment and response surface experiment, the effects of soaking temperature, soaking time, germination temperature, germination time and soaking liquid CaCl₂ concentration on the polyphenol content of mung bean were analyzed. The optimal germination conditions of mung bean were determined as soaking temperature 25°C, soaking time 11 h, germination temperature 28°C, germination time 3 days and CaCl₂ concentration 2 mM. Under these conditions, the content of polyphenol extract in germinated mung bean was 4.878 ± 0.30 mg/g, which was 3.07 times higher than that in ungerminated mung bean. The structure and content of purified polyphenols in germinated mung bean were determined by HPLC-MS/MS. Quinic acid, Quercetin, Rutin, Vitexin, Isovitexin and other substances were identified, and the content of polyphenols was 65.19%. In addition, through the in vivo and in vitro hypoglycemic activity experimental study of germinated mung bean polyphenols extract, the results showed that germinated mung bean polyphenols had an in vitro inhibitory effect on α-glucosidase, IC₅₀ was 44.45 mg/ml. In vitro inhibitory activity was stronger after digestion. Polyphenol extract can significantly reduce blood sugar and improve insulin resistance in Type 2 diabetic mice (T2DM). According to the results, germination treatment is an effective way to increase the content of polyphenols in mung bean, and the polyphenols extract has hypoglycemic activity.

Dipeptidyl peptidase IV (DPP-IV) inhibitory peptides have emerged as promising functional ingredients for managing type 2 diabetes due to their ability to enhance insulin secretion and improve glycemic control. This review provides a concise overview of current strategies for the preparation and encapsulation of DPP-IV inhibitory peptides, with a focus on food industry application, evaluating bioinformatics for substrate selection, and methods like mild enzymatic hydrolysis, cost-effective fermentation, and high-purity chemical synthesis for peptide production. Challenges associated with incorporating these peptides into food products are addressed, including impacts on sensory properties, stability during processing and digestion, and the need for effective delivery systems to enhance bioavailability. Potential solutions to improve peptide stability and targeted release, such as emulsions, liposomes, and nanoparticles, are explored. Future research directions are outlined, emphasizing the necessity for scalable production methods, co-encapsulation strategies, and consumer acceptance studies to facilitate the commercialization of DPP-IV inhibitory peptides as functional food ingredients. By addressing these key areas, this review aims to provide a theoretical foundation and practical guidance for the development of DPP-IV inhibitory peptides, paving the way for their broader application in the prevention and management of type 2 diabetes.