Use of Castanets (Terminalia catappa Linn) in the production of pectinases and cellulases by Solid State Fermentation (FES) using Aspergilus niger IOC 3998 and use of its bioactive compounds
Terminalia catappa Linn, bioactive compounds, enzyme inhibition, nanoemulsion, polygalacturonase, cellulases, solid state fermentation
Abstract: Castanets (Terminalia catappa Linn) are edible but have no commercial value. In this context, the present study investigated the potential of the castannet fruit for the development of extract with bioactive properties aiming to inhibit the α-amylase enzyme and its use in cosmetics. In addition, the fruit was also used as a substrate for obtaining pectinases and cellulae from solid state fermentation (FES). The pulp extracts showed values of phenolic compounds (2.984mg/g ± 0.38), flavonoids (1.644mg/g ± 0.21), flavonols (0.123mg/g ± 0.001) and total anthocyanins (0.505mg/g ± 0.21) 0.09) and inhibition of α-amylase enzyme reaching 100% with concentrated extract. For the encapsulation by nanoemulsions, using distilled water as the aqueous phase, Crodamol OQ-LQ as the oil phase and Tween 80 as the emulsifier, it was verified the formation of 3 systems with mean diameters 43.2 nm ± 0.6 for the F1. 41.1 nm ± 0.3 for F2 and 68.9 nm ± 0.3 for F3. The best values found in the fermentation process for polygalacturonase and pectin lyases were 32.61 U/g (30°C, pH 8.0 and 80% humidity) and 189.91 U/g (30°C, pH 4.0 and 80% humidity), respectively. In the factorial design, pH contributions and temperature-pH and temperature-humidity interactions were significant for PG. While for PMGL, moisture and temperature-pH interaction were significant. The enzymatic extracts of PG and PMGL were stable at temperatures between 30 and 70°C. However, the extracts were not very stable (40% of relative activity) at different pHs for PG, and for PMGL it remained stable (100 to 70% of relative activity) up to 1h of incubation. The treated residue had the best yield (22%), with CMCase and FPase production of 13.2 U/g and 0.232 U/g respectively. The enzymatic extracts performed better at neutral pH and at temperatures above 50 °C the enzymatic activity decreased to 37.18% and 18.48% respectively.