Artocarpus altilis extracts as a food-borne pathogen and oxidation inhibitors: RSM, COSMO RS, and molecular docking approaches.

Lipid oxidation and microbial contamination are the major factors contributing to food deterioration. Food additives like antioxidants and antibacterials can prevent food spoilage by delaying oxidation and preventing the growth of bacteria. Artocarpus altilis leaves exhibited biological properties that suggested its use as a new source of natural antioxidant and antimicrobial. Supercritical fluid extraction (SFE) was used to optimize the extraction of bioactive compounds from the leaves using response surface methodology (yield and antioxidant activity). The optimum SFE conditions were 50.5 °C temperature, 3784 psi pressure and 52 min extraction time. Verification test results (Tukey's test) showed that no significant difference between the expected and experimental DPPH activity and yield value (99%) were found. Gas-chromatography -mass spectrometry (GC-MS) analysis revealed three major bioactive compounds existed in A. altilis extract. The extract demonstrated antioxidant and antibacterial properties with 2,3-diphenyl-1-picrylhydrazyl (DPPH) scavenging activity, ferric reducing ability of plasma (FRAP), hydroxyl radical scavenging activity, tyrosinase mushrrom inhibition of 41.5%, 8.15 ± 1.31 (µg of ascorbic acid equivalents), 32%, 37% and inhibition zone diameter of 0.766 ± 0.06 cm (B. cereus) and 1.27 ± 0.12 cm (E. coli). Conductor like screening model for real solvents (COSMO RS) was performed to explain the extraction mechanism of the major bioactive compounds during SFE. Molecular electrostatic potential (MEP) shows the probability site of nucleophilic and electrophilic attack during bacterial inhibition. Based on molecular docking study, non-covalent interactions are the main interaction occurring between the major bioactive compounds and bacteria (antibacterial inhibition).

The applicability of using a protease extracted from cashew fruits (Anacardium occidentale), as possible meat tenderizer: An experimental design approach.

Meat tenderness is one of the most important organoleptic properties in determining consumer acceptance in meat product marketability. Therefore, an effective meat tenderization method is sought after by exploring plant-derived proteolytic enzymes as meat tenderizer. In this study, a novel protease from Cashew was identified as a new alternative halal meat tenderizer. The extraction of cashew protease was optimized using response surface methodology (R2 = 0.9803) by varying pH, CaCl2 concentration, mixing time, and mass. pH 6.34, 7.92 mM CaCl2 concentration, 5.51 min mixing time, and 19.24 g sample mass were the optimal extraction conditions. There was no significant difference (n = 3; p < 0.05) between the calculated (6.302 units/ml) and experimental (6.493 ± 0.229 units/ml) protease activity. The ascending order of the effects was pH < mixing time < CaCl2 < sample mass. In meat tenderizing application, the meat samples treated with 9% (v/w) crude protease extract obtained the lowest shear force (1.38 ± 0.25 N) to cause deformation on the meat. An electrophoretic analysis showed that protein bands above ~49.8 kDa were completely degraded into protein bands below ~22.4 kDa. Scanning electron microscopy shows the disruption of the muscle fibers after being treated by the Cashew protease. The results of this study show the Cashew (Anacardium occidentale) crude extract can be used as an alternative of the animal and microbial protease as meat tenderizer and subsequently overcome the shortcoming of the halal industrial protease.