Fei Liu

Pandan (Pandanus amaryllifolius), a tropical aromatic plant, is a rich source of lipophilic bioactive compounds, notably characterized by high levels of squalene, phytol, and β-sitosterol, which exhibit antioxidant and lipid-lowering effects. Bovine milk proteins (α-casein, β-casein, and β-lactoglobulin) are widely used as delivery matrices owing to their nutritional value and technological functionality. In this study, molecular docking, fluorescence spectroscopy, circular dichroism spectroscopy, Fourier-transform infrared spectroscopy, and an in vitro digestion model were employed to systematically investigate the interactions between the major lipophilic bioactive compounds from pandan and bovine milk proteins. The results demonstrated that these compounds bound to milk proteins through hydrophobic interactions and van der Waals forces, resulting in the formation of protein–ligand complexes. Such interactions induced distinct conformational changes in the proteins, with caseins adopting a more compact structure, whereas β-lactoglobulin underwent localized unfolding. Furthermore, in vitro digestion revealed that the protein–bioactive systems exhibited distinct digestion-stage-dependent DPPH• and ABTS•+ radical-scavenging capacities, with the complexes displaying phase-dependent radical-scavenging responses during both gastric and intestinal phases. These findings provide molecular-level insights into the interactions between pandan bioactives and milk proteins and provide a theoretical basis for developing functional dairy products enriched with pandan-derived ingredients.

With the growing interest in pandan-based products, bitterness and astringency associated with flavonoids may limit their sensory acceptance. This study investigated the interactions and taste-modulating effects of two milk proteins, β-casein (β-CN) and β-lactoglobulin (β-LG), with two representative bitter flavonoids, catechin (C) and naringin (NAR), in aqueous model systems. Fluorescence spectroscopy showed that both flavonoids produced concentration-dependent quenching of the milk proteins. β-CN exhibited more pronounced interaction-related spectroscopic responses than β-LG, which may be associated with its flexible and intrinsically disordered structure. Molecular docking predicted hydrogen-bonding and hydrophobic interactions in all four protein–flavonoid systems, with catechin and naringin interacting mainly with the internal hydrophobic cavity of β-LG and surface-exposed regions of the β-CN model. Circular dichroism and Fourier-transform infrared spectroscopy indicated ligand-dependent structural changes. For β-LG, catechin slightly decreased the estimated antiparallel and total β-sheet fractions, whereas naringin produced a modest increase. For β-CN, catechin produced a more apparent redistribution between the estimated α-helix and β-sheet fractions, while naringin caused comparatively smaller changes. Electronic tongue measurements showed that the addition of the milk proteins reduced the bitterness- and astringency-related sensor responses of catechin and naringin. Under the tested conditions, β-CN produced greater attenuation of these responses than β-LG, while the umami-related response remained comparatively high. These findings support the potential application of milk proteins as taste-modulating components in flavonoid-containing dairy formulations, although validation in real food matrices is required.

Cocoa pod husk is the main byproduct of cocoa processing and is rich in pectin, holding great potential for high–value utilization. Traditional acid extraction causes severe environmental pollution, while the single enzymatic method is time–consuming, necessitating the development of a green and efficient extraction technology. In this study, an ultrasound–assisted enzymatic extraction method was employed, and the extraction process was systematically optimized via Plackett–Burman design, the steepest ascent method, and Box–Behnken response surface methodology. Under the optimized conditions, the pectin yield, galacturonic acid content, and degrees of esterification were 14.34 ± 0.39%, 67.93 ± 1.13%, and 43.62 ± 0.6%, respectively, indicating low–methoxyl pectin characteristics. Compared with literature data, the present method showed favorable performance in terms of yield, purity, extraction time, and enzyme consumption relative to conventional acid and single enzymatic extraction methods. This approach effectively couples ultrasonic cell wall disruption with specific enzymatic hydrolysis, thereby enabling efficient preparation of high–quality pectin under mild, low–energy conditions. It provides a green and highly efficient alternative for the resource utilization of cocoa pod husk waste.

As an important carrier of East Asian dietary culture, the unique flavor and quality of fermented bean paste directly affect its market competitiveness. However, previous studies have primarily focused on microbial communities or overall flavor components, and there is still a lack of comprehensive understanding of the systematic correlation and dynamic regulation mechanisms between the two. The scientific elucidation and precise regulation of the microbial–metabolic network during the fermentation process have become critical challenges facing the industry today. Based on current research on the flavor, microbial community, and flavor‐related pathways of fermented bean paste, this review provides a systematic framework integrating microbial communities, flavor formation, and intelligent regulation technologies. It systematically elaborates on the spatiotemporal heterogeneity of microbial communities during fermented bean paste fermentation, clarifying how core functional microbiota drive flavor synthesis through stage‐specific metabolic activities. Furthermore, it discusses the application potential of synthetic microbial communities and digital twin technology in the precise monitoring of fermentation and targeted regulation of flavor. This review aims to provide theoretical support for the standardization and intelligent upgrading of fermented bean paste production processes, thereby promoting the development of the fermented bean paste industry toward high quality, high efficiency, and intelligence.

Creating effective treatments for type 2 diabetes mellitus (T2DM) remains a critical global health challenge. This study investigates the antidiabetic mechanisms of Bifidobacterium longum subsp. longum B-53 (B. longum B-53) in T2DM mice. Results showed that B. longum B-53 improved glucose homeostasis, reducing hemoglobin A1c from 317.2 ± 8.8 nmol/L to 168.3 ± 6.4 nmol/L and decreasing oral glucose tolerance test AUC (p < 0.05). B. longum B-53 outperformed metformin in regulating lipids and reducing weight, low-density lipoprotein cholesterol, total cholesterol, and triglycerides while increasing HDL-C. Systemic inflammation was reduced with elevated interleukin-10 (p < 0.05). B. longum B-53 improved the intestinal barrier function, decreased oxidative stress, ameliorated hepatic steatosis, and raised insulin levels. Mechanistically, B. longum B-53 reshaped gut microbiota, enriched indole metabolites, activated AhR/GLP-1/PDX-1 signaling to boost GLP-1 secretion, and regulated hepatic InsR/PI3K/Akt and AMPK/SREBP-1c pathways for glucose/lipid metabolism. These findings support B. longum B-53 as a promising functional food for metabolic disorders.