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A novel feruloyl esterase from a soil metagenomic library with tannase activity

Yao, Jian, Chen, Qing Long, Shen, Ai Xi, Cao, Wen, Liu, Yu Huan
Journal of Molecular Catalysis. B, Enzymatic 2013 v.95 pp. 55-61
Escherichia coli, amino acids, ammonium compounds, catalytic activity, cotton, epicatechin, epigallocatechin, feruloyl esterase, genes, genomic libraries, magnesium, manganese, molecular weight, nickel, pH, screening, sequence analysis, soil, tannase, tannins, temperature
A gene (tan410) encoding a feruloyl esterase was isolated by screening a cotton soil metagenomic library. Sequence analysis revealed that tan410 encodes a protein of 520 amino acids with a predicted molecular weight of 55kDa. The gene was further expressed in Escherichia coli BL21 (DE3) using a pET expression system. The recombinant enzyme was purified and characterized. Its optimum temperature and pH were 35°C and 7.0, respectively. Tan410 activity was enhanced by the addition of Mn2+, Mg2+, NH4+ and Ni2+. Besides ethyl ferulate, methyl caffeate, and methyl p-coumarate, Tan410 can also hydrolyze methyl gallate, tannic acid, epicatechin gallate, and epigallocatechin gallate which makes Tan410 an interesting enzyme for biotechnological applications.