Solid-state fermentation for the production of biomass valorizing feruloyl esterase

Aspergillus niger ATCC 13497 has been used to produce feruloyl esterase type A enzyme. The process parameters were optimized to attain a maximum of 11984.1 U/gds of enzyme activity within a period of 72 h using destarched wheat bran as a substrate. The purified enzyme studied in the present work displays a pH optimum of 5, and a temperature optimum of 37 °C. The enzyme has a size of 35 kDa and exhibited moderate thermostability, with 41% of activity retained at 90 °C. Ni +2 and Co+2 ions were found to have stimulatory activity on the enzyme with 66% and 78% increase in activity respectively. Cu+2 inhibited the activity by 88%. Statistical optimization enhanced the enzyme activity by 2.47 fold.