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Indonesia has plant-based traditional medicine (herbal) that is hereditary and believed to be used for disease therapy and prevention. The well-known of this traditional medicine is jamu, which has a long history of making, and now, some have limitedly explored their benefits on health scientifically. Traditional herbal drinks are part of jamu and are usually consumed as beverages for leisure and refreshment; in addition, they are hereditary believed to have many health benefits. The health efficacy of these herbal drinks is still poorly explored scientifically. This review explores the diversity, preparation methods, and health benefits of the most popular Indonesian traditional herbal drinks, mainly in Java Island, including kunyit asam, beras kencur, sinom, wedang uwuh, wedang jahe, and wedang pokak. Combining a literature review with field observations, it highlights key bioactive compounds such as curcumin, gingerol, and brazilin, known for their antioxidant, anti-inflammatory, and antimicrobial properties. The study uniquely integrates traditional knowledge with insights into modern processing techniques, such as ultra-high temperature processing by small-scale enterprises, and examines their cultural and historical significance. By addressing the limited scientific exploration of these drinks' health benefits, this paper bridges the gap between traditional practices and scientific validation, contributing to the global understanding of functional beverages. Modern adaptations, including ultra-high temperature processing by small-scale enterprises, have enabled wider distribution and commercialization of herbal drinks. However, challenges such as maintaining bioactive compound integrity and scaling production while preserving traditional authenticity remain critical. [ABSTRACT FROM AUTHOR]

Liberica coffee has an inferior quality when compared to arabica and robusta coffee. This flavour can be improved through a fermentation process involving indigenous microbes, one of which is a group of pectinolytic yeasts. Therefore, this study aimed to obtain yeast isolates with pectinolytic activity. Green bean samples were used for yeast isolation using YEPD agar media. Selected yeast isolates were screened for their pectinolytic activity semi-quantitatively using the well-diffusion method and quantitatively using the dinitrosalicylic acid (DNS) method. A total of six yeast isolates with different colony morphological characters were obtained and referred to as isolates Y1, Y2, Y3, Y4, Y5, and Y6. The isolates suspected to produce pectinase enzyme due to a clear zone around the well are Y2, Y3, Y4, and Y5. Y5 had the highest pectinolytic index, 022 and 0,73 on the second and fifth days of incubation, respectively. The four selected isolates were then screened quantitatively and showed that Y2 had the highest pectinase enzyme activity with a value of 12,66 ± 0,17 U/mL. The results showed that four yeast isolates from Liberica green coffee beans had pectinolytic activity with the highest enzyme activity found in Y2.

Background/Objectives: Type 2 diabetes (T2D) has become a critical global health issue, with an increasing prevalence that contributes to significant morbidity and mortality. Inhibiting dipeptidyl peptidase-IV (DPP4) is a promising strategy for managing T2D. This study aimed to explore the DPP4 inhibitory peptide derived from bitter melon seed protein (BMSP) hydrolysate. Methods: Reversed-phase high-performance liquid chromatography (RP-HPLC) was utilized to fractionate the hydrolysate. Peptide in the highest activity fraction was analyzed using liquid chromatography-mass spectrometry (LC-MS/MS). Peptide synthetic was used for further characterizations, such as bioactivity exploration, inhibition mechanism, molecular docking, and peptide stability against in vitro simulated gastrointestinal (SGI) digestion. Results: The BMSP hydrolysate was digested with gastrointestinal proteases (GP) and assessed for DPP4 inhibitory activity, yielding an IC50 of 1448 ± 105 μg/mL. Following RP-HPLC fractionation, MPHW (MW4) and VPSGAPF (VF7) were identified from fraction F8 with DPP4 IC50 values of 128.0 ± 1.3 µM and 150.6 ± 3.4 µM, respectively. Additionally, MW4 exhibited potential antihypertensive effects through ACE inhibition with an IC50 of 172.2 ± 10.6 µM. The inhibitory kinetics and molecular docking simulations indicated that both MW4 and VF7 were competitive inhibitors of DPP4, while MW4 was also a competitive inhibitor of ACE. Importantly, both peptides remained stable during simulated gastrointestinal digestion, suggesting their resistance to human digestive processes and their capacity to maintain biological activity. Conclusions: The findings suggest that BMSP-GP hydrolysate may have potential in terms of the development of health foods or therapeutic agents. However, in vivo studies are also essential for further confirmation of efficacy. [ABSTRACT FROM AUTHOR]

The loss of fresh produce along the supply chain represents a significant contributor to environmental and economic burden. Although technological advances in distribution and storage have provided a means to reduce the loss of fresh produce, in resource-limited settings, these technologies may not be available. One attractive approach to help address this limitation is to use edible coatings to protect fresh produce from biotic and abiotic factors that cause food deterioration. Here, we developed edible coatings from materials that are cheap and easy to prepare: maize starch, κ-carrageenan, and agar as the matrix; glycerol as the plasticizer; and Lactobacillus plantarum TPB21.12 as the active ingredient. Using fresh cut apples as a model substrate, we found that maize starch coating retained color, agar coating delayed browning, and κ-carrageenan coating decreased mass shrinkage of the fresh cut apples. L. plantarum TPB21.12 remained viable in the edible coating suspensions during storage and was active against Escherichia coli TPB21.8, a model bacterium for biotic factor that causes food spoilage. The simplicity of the edible coating formulation and preparation method offers an attractive approach for applications to help protect fresh produce from deterioration and reduce food loss and waste generation. [ABSTRACT FROM AUTHOR]

Plants have evolved many strategies to protect themselves from attack, including peptide toxins that are ribosomally synthesized and thus adaptable directly by genetic polymorphisms. Certain toxins in Clitoria ternatea (butterfly pea) are cyclic cystine-knot peptides of c. 30 residues, called cyclotides, which have co-opted the plant's albumin-1 gene family for their production. How butterfly pea albumin-1 genes were commandeered and how these cyclotides are utilized in defence remain unclear. The role of cyclotides in host plant ecology and biotechnological applications requires exploration., We characterized the sequence diversity and expression dynamics of precursor and processing proteins implicated in butterfly pea cyclotide biosynthesis by expression profiling through RNA-sequencing ( RNA-seq). Peptide-enriched extracts from various organs were tested for activity against insect-like membranes and the model nematode Caenorhabditis elegans., We found that the evolution and deployment of cyclotides involved their diversification to exhibit different chemical properties and expression between organs facing different defensive challenges. Cyclotide-enriched fractions from soil-contacting organs were effective at killing nematodes, whereas similar enriched fractions from aerial organs contained cyclotides that exhibited stronger interactions with insect-like membrane lipids., Cyclotides are employed as versatile and combinatorial mediators of defence in C. ternatea and have specialized to affect different classes of attacking organisms. [ABSTRACT FROM AUTHOR]