Angelica keiskei contains a variety of bioactive compounds including chalcone, coumarin, and phytochemicals, endowing it with pharmacological effects such as lipid-lowering activity, antitumor activity, liver protection, and nerve protection. This study aims to study the hypoglycemic and hypolipidemic effects of the flavonoid-rich extract from Angelica keiskei (FEAK) in an effort to exploit new applications of FEAK and increase its commercial value. In this paper, flavonoid compounds in Angelica keiskei were extracted using 50% ethanol, and the contents of the flavonoid compounds were analyzed by UPLC-MS/MS. Then, the hypoglycemic and hypolipidemic activities of the FEAK were investigated through in vitro enzyme activity and cell experiments as well as establishing in vivo zebrafish and Caenorhabditis elegans (C. elegans) models. The UPLC-MS/MS results show that the major flavonoid compounds in the FEAK were aureusidin, xanthoangelol, kaempferol, luteolin, and quercetin. The inhibitory rates of the FEAK on the activity of α-amylase and cholesterol esterase were 57.13% and 72.11%, respectively. In cell lipid-lowering experiments, the FEAK significantly reduced the total cholesterol (TC) and total triglyceride (TG) levels in a dose-dependent manner, with 150 μg/mL of FEAK decreasing the intracellular levels of TC and TG by 33.86% and 27.89%, respectively. The fluorescence intensity of the FEAK group was 68.12% higher than that of the control group, indicating that the FEAK exhibited hypoglycemic effects. When the concentration of the FEAK reached 500 μg/mL, the hypoglycemic effect on zebrafish reached up to 57.7%, and the average fluorescence intensity of C. elegans in the FEAK group was 17% lower than that of the control group. The results indicate that the FEAK had hypoglycemic and hypolipidemic activities. The findings of this study provide theoretical references for the high-value utilization of Angelica keiskei and the development of natural functional food with hypoglycemic and hypolipidemic activities.
Myofibrillar proteins (MPs) are important to the gel formation that occurs in frozen surimi. Importantly, their unique gel‐forming ability indicates that surimi may be a promising material for use in 3D printing. The objective of the present study was to investigate the effects of collagen peptides on the cryoprotection of MPs during freeze–thaw (FT) cycles and the subsequent printability of surimi. The results showed that the collagen peptide had both protective and destructive actions during the tested FT cycles. The addition of 1.0% collagen peptide provided significant cryoprotection to the MPs. This addition effectively maintained the structural stability of MPs while also weakening FT effects on bound water and its mobility. We also assessed the rheological and 3D‐printing characteristics of surimi with 1.0% collagen peptide. The rheological results indicated that the surimi with collagen peptides had better characteristics, including shear‐thinning behavior, better recovery, and improved mechanical properties. Combined with the actual printing effect, materials with good shear‐thinning behavior, high apparent viscosity, and high recovery might be more suitable for 3D printing. Moreover, the high G′ contributed to good structural maintenance after printing. Collectively, these results indicated that collagen peptide may serve as a new, low‐sugar cryoprotectant for use in surimi. Moreover, that its use would result in a healthier system that has increased stability, precision, and formability with applications in extrusion‐based 3D printing. The results of this study provide theoretical reference for the development of new surimi materials with freezing stability and good 3D printing performance. Practical Application This study confirmed the protective action of 1.0% collagen peptides for surimi and the contribution of it to well printing precision and structure maintenance for 3D printing, providing a firm foundation for the use of collagen peptide as a low‐sugar cryoprotectant and developed a new type of surimi as a food material for 3D printing.
Flavonoids are easily destroyed and their activity lost during gastrointestinal digestion. Protein-based nanocomplexes, a delivery system that promotes nutrient stability and bioactivity, have received increasing attention in recent years. This study investigated the stability, inhibitory activity against α-glucosidase and interaction mechanisms of protein-based nanocomplexes combining whey protein isolate (WPI), soybean protein isolate (SPI) and bovine serum albumin (BSA) with flavonoids (F) from A. keiskei using spectrophotometry, fluorescence spectra and molecular docking approaches. The results show that the flavonoid content of WPI-F (23.17 ± 0.86 mg/g) was higher than those of SPI-F (19.41 ± 0.56 mg/g) and BSA-F (20.15 ± 0.62 mg/g) after simulated digestion in vitro. Furthermore, the inhibition rate of WPI-F (23.63 ± 0.02%) against α-glucosidase was also better than those of SPI-F (18.56 ± 0.02%) and BSA-F (21.62 ± 0.02%). The inhibition rate of WPI-F increased to nearly double that of F alone (12.43 ± 0.02%) (p < 0.05). Molecular docking results indicated that the protein-flavonoids (P-F) binding occurs primarily through hydrophobic forces, hydrogen bonds and ionic bonds. Thermodynamic analysis (ΔH > 0, ΔS > 0) indicated that the P-F interactions are predominantly hydrophobic forces. In addition, the absolute value of ΔG for WPI-F is greater (−30.22 ± 2.69 kJ mol−1), indicating that WPI-F releases more heat energy when synthesized and is more conducive to combination. This paper serves as a valuable reference for the stability and bioactivity of flavonoids from A. keiskei.
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