期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 61, 期 14, 页码 -出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202117324
关键词
Biocatalysis; Carboxylic Acids; Cascades; Enzymes; Methyltransferase
资金
- EPSRC
- Biocatnet/BBSRC
Carboxyl methyltransferase enzymes from Aspergillus fumigatus showed high regioselectivity and good conversions in methylating a broad range of aromatic mono- and dicarboxylic acids. The second methylation of dicarboxylic acids exhibited strong pH dependence, with an optimum at pH 5.5-6. Potential for industrial biotechnology application was demonstrated in the production of a bioplastics precursor from bioderived 5-hydroxymethylfurfural.
Carboxyl methyltransferase (CMT) enzymes catalyse the biomethylation of carboxylic acids under aqueous conditions and have potential for use in synthetic enzyme cascades. Herein we report that the enzyme FtpM from Aspergillus fumigatus can methylate a broad range of aromatic mono- and dicarboxylic acids in good to excellent conversions. The enzyme shows high regioselectivity on its natural substrate fumaryl-L-tyrosine, trans, trans-muconic acid and a number of the dicarboxylic acids tested. Dicarboxylic acids are generally better substrates than monocarboxylic acids, although some substituents are able to compensate for the absence of a second acid group. For dicarboxylic acids, the second methylation shows strong pH dependency with an optimum at pH 5.5-6. Potential for application in industrial biotechnology was demonstrated in a cascade for the production of a bioplastics precursor (FDME) from bioderived 5-hydroxymethylfurfural (HMF).
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据