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Moringa oleifera is a tropical plant in the Moringaceae family that contains a lot of bioactive compounds. This study aimed to isolate and characterize the enzyme xanthine oxidase (XO), and conducted inhibitory tests on XO using methanol extracts of M. oleifera leaves. The xanthine oxidase enzyme isolated from bovine milk was characterized to determine the optimum pH, temperature, and substrate concentration. XO inhibition was evaluated by in vitro and in silico methods. The results of XO isolation and characterization of bovine milk showed the optimum conditions at pH 6.5, substrate concentration of 0.1 mM, and temperature 35 °C with an activity rate of 32.47 mU/mL; 21.55 mU/mL, and 21.94 mU/mL. Inhibition analysis results on methanol extract of M. oleifera leaves showed the highest activity decrease at the extract concentration of 160 ppm, with a relative inhibition value of 21.35%, while allopurinol as a positive control has a relative value inhibition of 61.21%. Relative value inhibition indicated the potential of M. oleifera leaves as a source of medicinal plants for gout sufferers. Additionally, a computational analysis was performed to observe the molecular interaction between the primary compounds of M. oleifera leaves, i.e., 5-O-acetyl-thio-octyl-β-L-rhamnofuranoside, quinic acid, and 2-dimethyl(trimethylsilylmethyl)silyloxymethyltetrahydrofuran, and XO using the molecular docking method. The finding implied that these compounds are bound to the catalytic sites of XO by hydrogen bonds and hydrophobic interactions, indicating the primary compounds of M. oleifera leaves could become XO inhibitors to treat gout disease.

Nanotechnology explores nanoscale materials that can be used in a wide range of industries such as biotechnology, cosmetics, drug delivery, nanomedicine, and biosensors. Nanoparticles in diverse shapes and sizes can be prepared through physical, chemical, and biological methods. The employment of reducing agents, which will change their form, size range, level of stability, and interaction, is a crucial part thus employing a biological approach is necessary. Chemically generated metal oxide nanoparticles raise considerable issues owing to the usage of hazardous and poisonous chemicals, as well as the potential for conservational impairment. In contrast, the production of silver nanoparticles using the principal method of green synthesis has found a special place in research that is considered more environmentally approachable requiring the use to produce non-toxic nanomaterials. Plants and polymer materials have received a lot of interest in the preparation of nanoparticles since they are renewable and affordable. In this review, we present a comprehensive overview of more ecologically friendly synthesis techniques that use plant extracts to make silver nanoparticles and their application as antibacterial agents, as well as toxicity features based on the shape, size range, and phytochemical mechanism of plants.

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Thermostable amylase enzyme has a broad commercial value in its use in the processing of starch, sugar production, textile, paper, animal feed, pharmaceuticals and in the manufacture of detergents. This study aims to determine the optimum conditions of amylase production from the termofil bacteria Bacillus sp. RSII-1b isolated from a hot spring Lejja South Sulawesi and characterizing the amylase enzyme. The testing of amylase production was done with various concentration of starch and CaCl 2 in the production medium, then fermented to obtain maximum amylase activity, amylase enzyme was produced in optimum condition, and its characteristic was tested using 2% starch substrates in various pH, temperature and determining the compound cofactor which can act as activators or inhibitors of the amylase activity, the enzyme activity was tested using DNS method. Crude extract enzyme has the highest enzyme activity of the protein content determined by the method of Lawry. The results showed that the amylase enzyme from Bacillus sp RSAII-1b isolates can be manufactured to a maximum at 33 hours of fermentation time with conditions: the concentration of substrate (starch) 1.5%, 0.08% CaCl 2 , 55°C temperature, medium pH 7.0 and aeration speed 200rpm with the activity of 0.1323U/mL, amylase crude extract protein content of 1.86mg/mL, with spesifik activity 0.0711 U/mg protein. Crude extract amylase work optimally at pH 6.0; 55°C-60°C the amylase activity of 0.165U/mL, the specific activity of 0.089U/mg protein. Amylase enzyme is an enzyme that depends on metal because its catalytic activity can be activated by metal ions Ca 2+ , Mg 2+ , Cu 2+ , Ni 2+ and Co 2+ as activators whereas Zn 2+ ions decrease the activity of enzymes as inhibitors. Amylase activity in the crude extract optimum conditions with the addition of 10 mm ions Ca 2+ can increase amylase activity up to 32,89%, while the addition of ions Zn 2+ can inhibit amylase activity up to 25%.