Ferulic acid production from wheat bran by integration of enzymatic pretreatment and a cold-adapted carboxylesterase catalysis

High-value chemical production from natural lignocellulose transformation is a reliable waste utilization approach. A gene encoding cold-adapted carboxylesterase in Arthrobacter soli Em07 was identified. The gene was cloned and expressed in Escherichia coli to obtain a carboxylesterase enzyme with a molecular weight of 37.2 KDa. The activity of the enzyme was determined using & alpha;-naphthyl acetate as substrate. Results showed that the optimum enzyme activity of carboxylesterase was at 10 degrees C and pH 7.0. It was also found that the enzyme could degrade 20 mg enzymatic pretreated de-starched wheat bran (DSWB) to produce 235.8 & mu;g of ferulic acid under the same conditions, which was 5.6 times more than the control. Compared to the chemical strategy, enzymatic pretreatment is advantageous because it is environmentally friendly, and the by-products can be easily treated. Therefore, this strategy provides an effective method for high-value utilization of biomass waste in agriculture and industry.

Automated summary

A gene encoding cold-adapted carboxylesterase in Arthrobacter soli Em07 was cloned and expressed in Escherichia coli, resulting in a carboxylesterase enzyme with a molecular weight of 37.2 KDa. The enzyme exhibited optimum activity at 10 degrees C and pH 7.0. Under the same conditions, the enzyme could degrade 20 mg of enzymatic pretreated de-starched wheat bran (DSWB) to produce 235.8 µg of ferulic acid, which was 5.6 times more than the control. Compared to chemical strategies, enzymatic pretreatment is environmentally friendly and the by-products are easily treated, providing an effective method for high-value utilization of biomass waste in agriculture and industry.