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Hydrothermal carbonization (HTC) has recently emerged as a promising technology for converting diverse forms of waste with a high moisture content into value-added products such as biofuel, biochar, and activated carbon. With an increasing demand for sustainable and carbon-neutral energy sources, HTC has attracted considerable attention in the literature. However, a successful transition from laboratory-scale to large-scale industrial applications entails notable challenges. This review critically assesses the upscaling of hydrothermal carbonization processes, emphasizing the challenges, innovations, and environmental implications associated with this transition. The challenges inherent in upscaling HTC are comprehensively discussed, including aspects such as reactor design, process optimization, and the current treatment technology for process water. This review presents recent innovations and technological advancements that address these challenges and explores integrated solutions to enhancing hydrothermal carbonization’s scalability. Additionally, this review highlights key companies that have developed and implemented HTC plants for commercial purposes. By overcoming the obstacles and achieving advancements in the upscaling of hydrothermal carbonization, this review contributes to the ongoing efforts to realize the full potential of HTC as a sustainable and scalable biomass conversion technology and proposes future directions.

Obesity, characterized by excessive adipose tissue accumulation, has emerged as a crucial determinant for a wide range of chronic medical conditions. The identification of effective interventions for obesity is of utmost importance. Widely researched antiobesity agents focus on pancreatic lipase, a significant therapeutic target. This study presented the evaluation of ten flavonoid compounds in terms of their inhibitory activities against pancreatic lipase, utilizing both in vitro and in silico approaches. The results indicated that all tested compounds demonstrated modest and weaker inhibitory activities compared to the reference compound, orlistat. Among the compounds investigated, F01 exhibited the highest potency, with an IC50 value of 17.68 ± 1.43 µM. The enzymatic inhibition kinetic analysis revealed that F01 operated through a competitive inhibition mechanism with a determined Ki of 7.16 μM. This value suggested a moderate binding affinity for the pancreatic lipase enzyme. Furthermore, the associated Vmax value was quantified at 0.03272 ΔA·min−1. In silico studies revealed that F01 displayed a binding mode similar to that of orlistat, despite lacking an active functional group capable of forming a covalent bond with Ser152 of the catalytic triad. However, F01 formed a hydrogen bond with this crucial amino acid. Furthermore, F01 interacted with other significant residues at the enzyme’s active site, particularly those within the lid domain. Based on these findings, F01 demonstrates substantial potential as a candidate for further investigations.