The optimization of antioxidant and anti-tyrosinase activity during jellyfish hydrolysate preparation was studied using a response surface methodology (RSM) with a face-centered composite design. The influence of the hydrolysis duration and the enzyme concentration on the IC₅₀ of the DPPH and ABTS radical scavenging activity, ferric-reducing antioxidant power (FRAP), the degree of hydrolysis (DH), yield, and the IC₅₀ value of tyrosinase inhibitory activity were determined. The optimum conditions for the production of jellyfish hydrolysate using alcalase (JFAH), flavourzyme (JFFH), or papain (JFPH) were achieved at hydrolysis times of 360, 345, or 360 min, respectively, and at an enzyme concentration of 5.0%. JFFH had the highest antioxidant and tyrosinase inhibitory activity. JFAH, JFFH, and JFPH concentrations of 2.5 mg/mL resulted in HaCaT cells (IC₈₀) having a survival rate of 80%. The amino acid profile of JFFH contained about 43% hydrophobic and 57% hydrophilic amino acids, comprising Gly, Cys, Glx, Asx, which were dominant. The isolation of a peptide fraction from JFFH was carried out using ultrafiltration membranes (10, 3, and 1 kDa) and gel filtration chromatography. Fraction-III (1–3 kDa) showed the highest antioxidative and tyrosinase inhibitory activity.

This research aimed to enhance the physicochemical and antioxidant properties of dried whole longan fruit using Maillard reaction or non-enzymatic glycosylation (glycation) in a moist-dry-heating system at 60 °C with approximately 75% relative humidity for 5–50 days. During Maillard reaction, the browning index (BI) of the fruits increased significantly while lightless, redness and yellowness decreased. Interestingly, the rare sugars especially D-psicose and D-allose gradually increased by 2–3 folds when compared to the initial Maillard reaction. The development of D-mannose was additionally established through the glycation. The degree of glycation increased with the decrease of free amino acid, suggesting that conjugation of sugar with amino acids was involved. SDS-PAGE confirmed that the high molecular weight (HMW) of conjugated sugar-amino acid was the Maillard reaction product. The antioxidative properties including DPPH and ABTS radical scavenging activities, also ferric reducing antioxidant power (FRAP) were also increased as Maillard reaction progressed, which showed the activities in the range of 43.2–94.1 mg GAE/100 g dry basis, 0.23–3.09 g TE/100 g dry basis, and 0.35–5.95 g FeSO4/100 g dry basis, respectively. This study demonstrated a practical approach of Maillard reaction for the development of dried longan fruit with high antioxidative properties.

Herein, the possibility of valorizing defatted sesame seed meal (DSSM) as a viable source for valuable plant proteins and amyloid-based nanostructure was investigated. Sesame seed protein isolate (SSPI) and the major storage protein globulin (SSG) were prepared by alkaline extraction–isoelectric point precipitation as well as fractionation in the case of SSG. The protein samples were characterized for their physicochemical attributes. SSPI and SSG were also evaluated for their ability to form amyloid structures under heating (90 °C) at low pH (2.0). Additionally, the functional attributes, antioxidant activity, and biocompatibility of the proteins and amyloid nanostructures were also examined. SSPI and SSG were both successfully prepared from DSSM. The data showed that the physicochemical attributes of both protein samples were quite similar, except for the fact that SSG was mostly composed of 11S globulin, as evinced by Tricine-SDS-PAGE analysis. TEM micrographs revealed that SSG was able to form curly-shaped fibrillar amyloid structures, whereas those derived from SSPI were mostly amorphous. Thioflavin-T assay and Tricine-SDS-PAGE analysis indicated that acidic heating promoted protein hydrolysis and self-aggregation of the hydrolyzed peptides into a β-sheet rich amyloid structure. Importantly, the amyloid preparations displayed commendable solubility, superior water and oil holding capacities, and antioxidant activity against DPPH and ABTS. The protein amyloid nanostructures were found to be non-toxic against RAW264.7 cells, HaCaT cells, and red blood cells. These findings indicate that DSSM could be upcycled into valuable protein amyloid structures with good potentialities as novel food ingredients.

The sea cucumber body wall was subjected to enzymatic hydrolysis using papain. The relationship between the enzyme concentration (1–5% w/w protein weight) and hydrolysis time (60–360 min) and the degree of hydrolysis (DH), yield, antioxidant activities, and antiproliferative activity in a HepG2 liver cancer cell line was determined. The surface response methodology showed that the optimum conditions for the enzymatic hydrolysis of sea cucumber were a hydrolysis time of 360 min and 4.3% papain. Under these conditions, a 12.1% yield, 74.52% DH, 89.74% DPPH scavenging activity, 74.92% ABTS scavenging activity, 39.42% H₂O₂ scavenging activity, 88.71% hydroxyl radical scavenging activity, and 9.89% HepG2 liver cancer cell viability were obtained. The hydrolysate was produced under optimum conditions and characterized in terms of its antiproliferative effect on the HepG2 liver cancer cell line.

This study aimed to compare the efficiency of four extraction methods, hot water (HW), hot alkaline (HA), ultrasound-assisted water (UW), and ultrasound-assisted alkaline (UA), for extracting crude β-glucan from Lentinula edodes, focusing on yield, functionality, and antidiabetic potential. The response surface methodology was used to optimize extraction conditions. Among all methods, UW yielded the highest β-glucan content (34.51 ± 0.82 g/100 g dry extract), indicating enhanced extraction efficiency through acoustic cavitation. However, HW demonstrated the most preserved structural integrity, exhibiting superior and consistent swelling power across all tested pH conditions, which indicated an excellent water-holding capacity. The ability of HA to scavenge antioxidants was significantly higher than that of other methods, likely due to the enhanced release of phenolic residues under alkaline conditions. UA showed the most potent inhibition against α-amylase (IC₅₀ = 1.46 mg/mL) and α-glucosidase (IC₅₀ = 1.21 mg/mL), demonstrating the potential for type 2 diabetes management. These results highlight that while UW is optimal for yield, HW preserves functional integrity, HA enhances antioxidant properties, and UA is promising for enzyme inhibition. The findings provide insights into tailoring extraction strategies for targeted functional or nutraceutical applications.