A Protease-Insensitive Feruloyl Esterase from China Holstein Cow Rumen Metagenomic Library: Expression, Characterization, and Utilization in Ferulic Acid Release from Wheat Straw
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- 作者：Fansheng Cheng ; Jiping Sheng ; Ting Cai ; Jian Jin ; Wanzhen Liu ; Yanmei Lin ; Yongxin Du ; Maoqiu Zhang ; Lin Shen
- 刊名：Journal of Agricultural and Food Chemistry
- 出版年：2012
- 出版时间：March 14, 2012
- 年：2012
- 卷：60
- 期：10
- 页码：2546-2553
- 全文大小：532K
- 年卷期：v.60,no.10(March 14, 2012)
- ISSN：1520-5118
文摘
A metagenomic library of China Holstein cow rumen microbes was constructed and screened for novel gene cluster. A novel feruloyl esterase (FAE) gene was identified with a length of 789 bp and encoded a protein displaying 56% identity to known esterase sequences. The gene was functionally expressed in Escherichia coli BL21 (DE3), and the total molecular weight of the recombined protein was 32.4 kDa. The purified enzyme showed a broad specificity against the four methyl esters of hydroxycinnamic acids and high activity (259.5 U/mg) to methyl ferulate at optimum conditions (pH 8.0, 40 掳C). High thermal and pH stability were also observed. Moreover, the enzyme showed broad resistance to proteases. FAE-SH1 can enhance the release of ferulic acid from wheat straw with cellulase, 尾-1,4-endoxylanase, 尾-1,3-glucanase, and pectase. These features suggest FAE-SH1 as a good candidate to enhance biomass degradation and improve the health effects of food and forage.