The faeA genes from Aspergillus niger and Aspergillus tubingensis encode ferulic acid esterases involved in degradation of complex cell wall polysaccharides
The faeA genes from Aspergillus niger and Aspergillus tubingensis encode ferulic acid esterases involved in degradation of complex cell wall polysaccharides
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DOI：
10.1128/aem.63.12.4638-4644.1997
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发表时间：
1997-12-01
影响因子：
4.4
通讯作者：
Visser, J
中科院分区：
文献类型：
--
作者：
deVries, RP;Michelsen, B;Visser, J
我们报告了来自黑曲霉和塔宾曲霉的编码阿魏酸酯酶 faeA 的基因的克隆和表征。黑曲霉和图宾曲霉基因具有高度的序列同一性，并含有一个保守的内含子。该基因产物 FAEB 在野生型塔宾曲霉和蛋白酶缺陷型黑曲霉突变体中过表达。这两个基因在野生型塔宾曲霉和黑曲霉蛋白酶缺陷突变体中的过表达表明，塔宾曲霉基因产物比来自黑曲霉的同等基因产物对降解更敏感。根据分子质量、最佳 pH 值和温度、pI、N 末端序列以及对阿魏酸甲酯的活性进行评估，来自黑曲霉的 FAEA 与黑曲霉 FAE-III (C. B. Faulds 和 G. Williamson, Microbiology 140:779-787, 1994) 相同。 faeA 基因通过在小麦阿拉伯木聚糖和甜菜果胶上生长而被诱导，其基因产物（FAEA）从小麦阿拉伯木聚糖中释放出阿魏酸。木聚糖酶的存在提高了释放速率。 FAEA 还从甜菜果胶中水解少量阿魏酸，但添加内果胶裂解酶几乎不会影响水解速率。
We report the cloning and characterization of a gene encoding a ferulic acid esterase, faeA, from Aspergillus niger and Aspergillus tubingensis. The A. niger and A. tubingensis genes have a high degree of sequence identity and contain one conserved intron. The gene product, FAEB, was overexpressed in wild-type A. tubingensis and a protease-deficient A. niger mutant. Overexpression of both genes in wild-type A. tubingensis and an A. niger protease-deficient mutant showed that the A. tubingensis gene product is more sensitive to degradation than the equivalent gene product from A. niger. FAEA from A. niger was identical to A. niger FAE-III (C. B. Faulds and G. Williamson, Microbiology 140:779-787, 1994), as assessed by molecular mass, pH and temperature optima, pI, N-terminal sequence, and activity on methyl ferulate. The faeA gene was induced by growth on wheat arabinoxylan and sugar beet pectin, and its gene product (FAEA) released ferulic acid from wheat arabinoxylan. The rate of release was enhanced by the presence of a xylanase. FAEA also hydrolyzed smaller amounts of ferulic acid from sugar beet pectin, but the rate was hardly affected by addition of an endo-pectin lyase.