Ahmed_2023_Sci.Rep_13_16755

Bioconversion using fungi, as natural factory of many applicable bioactive compounds, as enzymes utilizing agro-residue substrates as a solid, abundant, low-cost growth and enzyme production media. This study characterized and applied a tannase enzyme (308 U/mg) from Aspergillus niger A8 + Trichoderma viride co-cultures utilizing pomegranate peels. The partially purified enzyme showed maximal relative activity at 37-65 degreesC for 10 min and kinetics of thermal inactivation energy at a high point at 60 degreesC for 0.040/min. The half-life was 37 degreesC for 58.6 min, temperature coefficient Q(10) of tannase was maximal for 1.38 between 40 and 50 degreesC, and the activation energy was 17.42 kJ/mol. The enzyme activity peaked in the pH range of 4-8, and the maximum relative activity (100.6%) for tannase was achieved at pH 6. The K(m) and V(max) values for purified enzymes using tannic acid were 7.3 mg/mL and 3333.33 U/mL, respectively. The enzyme reduced the total tannin content in all tannin-rich substrates after 12h. The gallic acid (GA) had total phenols of 77.75 ppm and antioxidant activity of 82.91%. It was observed that the GA as antimicrobial influencer exhibited the largest inhibitory zone diameter (IZD) of 31 +/- 1.0 mm against Pseudomonas aeruginosa ATCC27853. The GA minimum inhibitory concentration value was ranged from 7770.0-121.41 microg/mL. The obtained GA showed a bactericidal effect against all bacterial strains except Shigella sonnei DSM5570 and Salmonella typhi DSM17058, which showed bacteriostatic behavior.