Department of Bioresource Engineering, Faculty of Agriculture, Yamagata University, Tsuruoka, Japan.
FEBS Lett. 2010 Sep 24;584(18):4032-6. doi: 10.1016/j.febslet.2010.08.021. Epub 2010 Aug 20.
In this study we report the biochemical characterization of a hypothetical protein from Aspergillus oryzae exhibiting sequence identity with feruloyl esterase and tannase from the genus Aspergillus. The purified recombinant protein showed a hydrolytic activity toward the ethyl, propyl, or butyl esters of 4-hydroxybenzoic acid, but did not show feruloyl esterase or tannase activity. Finally, the enzyme decreased the antimicrobial activity of parabens against A. oryzae via hydrolysis of the ester bond present in butyl 4-hydroxybenzoic acid.
在这项研究中,我们报告了米曲霉中一种假定蛋白的生化特性,该蛋白与米曲霉属的阿魏酸酯酶和单宁酶具有序列同源性。纯化的重组蛋白对 4-羟基苯甲酸的乙酯、丙酯或丁酯表现出水解活性,但没有表现出阿魏酸酯酶或单宁酶活性。最后,该酶通过水解丁基 4-羟基苯甲酸中的酯键,降低了对羟基苯甲酸酯对米曲霉的抗菌活性。