Introduction: Potentilla anserina (Potentilla anserina L.), also known as ginseng fruit, is a plant that can be used as both medicine and food. Potentilla anserina L. has high medical value in Chinese medicine, such as strengthening the spleen and stomach, replenishing qi and blood, and astringing hemostasis.Methods: In this study, polysaccharides of Potentilla anserina L. were extracted from the root using an enzyme-assisted extraction method. According to the principle of Box–Behnken design, response surface methodology was designed to optimize the extraction conditions. Fourier transform infrared spectroscopy and scanning electron microscopy were used to investigate the structure and appearance of Potentilla anserina L. polysaccharides. The monosaccharide composition of Potentilla anserina L. polysaccharides was determined using high-performance liquid chromatography. The antioxidant activities were also studied.Results: Under the optimal extraction conditions (the ratio of solid to liquid, 1:15; ratio of cellulase to pectinase, 1:2; extraction pH, 8.0; enzyme reaction temperature, 60°C), the extraction yield of Potentilla anserina L. polysaccharides was 19.80 ± 0.01%, equal to the model prediction value 19.84%. The data of Fourier transform infrared spectrum, scanning electron microscopy, and high-performance liquid chromatography showed that the Potentilla anserina L. polysaccharide was a kind of α-pyran polysaccharide, mainly consisting of galactose, glucose, rhamnose, and arabinose. The antioxidant results showed that Potentilla anserina L. polysaccharides had a strong hydroxyl radical scavenging ability (IC₅₀ = 0.367 mg/mL), superoxide anion scavenging ability (IC₅₀ = 45.017 mg/mL), and a certain degree of total reducing ability.Discussion: Enzyme-assisted extraction is an efficient method to extract Potentilla anserina L. polysaccharides. The Potentilla anserina L. polysaccharides could have potential use in functional foods as a natural antioxidant.

Lanzhou Lily (Lilium davidii var. unicolor) is a traditional medicinal plant and popular edible vegetable bulb in China. In this study, the polysaccharides of Lanzhou Lily (LLPs) were extracted by polyethylene glycol-based ultrasonic-assisted enzymatic extraction method (PEG-UAEE). The optimum process conditions were obtained by single-factor experiments and response surface methodology (RSM). Then, the preliminarily structure of LLPs was characterized by HPLC, FT-IR, and SEM, and its antioxidant activities were evaluated. The results showed that LLPs yield reached 14.75% under the optimized conditions: E/S ratio 1,400 U/g; pH 5.0, ultrasonic time 30 min; and ultrasonic temperature 50 °C. The LLPs has pyranoid ring, uronic acid, and the characteristic absorption peaks of -OH, C = O, and C-H. The results of scanning electron microscope indicated that the LLPs had irregular distribution, dispersed structure, and many holes. The HPLC analysis showed that the LLPs were heteropolysaccharide containing galactose (6.36%), glucose (76.03%), rhamnose (2.02%), and arabinose (7.09%). Moreover, the LLPs showed obvious antioxidant effect in vitro.

Chicken plasma protein hydrolysate (CPPH) was prepared by trypsin with angiotensin I‐converting enzyme (ACE) inhibitory activity of 53.5% ± 0.14% and the degree of hydrolysis (DH) of 16.22% ± 0.21% at 1 mg·ml⁻¹; then, five proteases, including pepsin, trypsin, papain, alcalase, and neutrase, were employed to improve ACE inhibitory ability by catalyzing plastein reaction. The results indicated that trypsin‐catalyzed plastein reaction showed the highest ACE inhibitory activity. The exogenous amino acids of leucine, histidine, tyrosine, valine, and cysteine were selected to modify the CPPH. The leucine‐modified plastein reaction released the highest ACE inhibitory activity. The effects of four reaction parameters on plastein reaction were studied, and the optimal conditions with the purpose of obtaining the most powerful ACE inhibitory peptides from modified products were obtained by response surface methodology (RSM). The maximum ACE inhibition rate of the modified hydrolysate reached 82.07% ± 0.03% prepared at concentration of hydrolysates of 30%, reaction time of 4.9 hr, pH value of 8.0, temperature of 40°C, and E/S ratio of 5,681.62 U·g⁻¹. The results indicated that trypsin‐catalyzed plastein reaction increased ACE inhibitory activity of chicken plasma protein hydrolysates by 28.57%.

Hepatocellular carcinoma (HCC) stands as the third leading cause of cancer-related fatalities globally. In this study, we observed a significant increase in the expression level of the YEATS2 gene in HCC patients, and it is negatively correlated with the patients' survival rate. While we have previously identified the association between YEATS2 and the survival of pancreatic cancer cells, the regulatory mechanisms and significance in HCC are still to be fully elucidated. Our study shows that knockdown (KD) of YEATS2 expression leads to DNA damage, which in turn results in an upregulation of γ-H2A.X expression and activation of the canonical senescence-related pathway p53/p21Cip1. Moreover, our transcriptomic analysis reveals that YEATS2 KD cells can enhance the expression of p21Cip1 via the c-Myc/miR-93-5p pathway, consequently fostering the senescence of HCC cells. The initiation of cellular senescence through dual-channel activation suggests that YEATS2 plays a pivotal regulatory role in the process of cell proliferation. Ultimately, our in vivo research utilizing a nude mouse tumor model revealed a notable decrease in both tumor volume and weight after the suppression of YEATS2 expression. This phenomenon is likely attributable to the attenuation of proliferative cell activity, coupled with a concurrent augmentation in the population of natural killer (NK) cells. In summary, our research results have supplemented the understanding of the regulatory mechanisms of HCC cell proliferation and indicated that targeting YEATS2 may potentially inhibit liver tumor growth.