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Thermostable feruloyl esterase for the bioproduction of ferulic acid from triticale bran

机译：用于从黑小麦糠中生物生产阿魏酸的热稳定阿魏酸酯酶

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摘要

A putative \u3b1/\u3b2 hydrolase fold-encoding gene (locus tag TTE1809) from the genome of Thermoanaerobacter tengcongensis was cloned and expressed in Escherichia coli as a possible source of thermostable feruloyl esterase (FAE) for the production of antioxidant phenolic acids from biomass. Designated as TtFAE, the 33-kDa protein was purified to apparent homogeneity. The lipase-like sequence characteristics of TtFAE and its substrate specificity towards methyl ferulate, methyl sinapate, and methyl p-coumarate classify it as a new member of the type A FAEs. At 75\ub0C, the enzyme retained at least 95% of its original activity for over 80 min; at 80\ub0C, its half-life was found to be 50 min, rendering TtFAE a highly thermostable protein. Under different hydrolytic conditions, ferulic acid (FA) was shown to be released from feruloylated oligosaccharides prepared from triticale bran. An estimated recovery of 68 mg FA/100 g triticale bran was demonstrated by a 30% release of the total FA from triticale bran within a 5-h incubation period. Both the oxygen radical absorbing capacity values of the feruloylated oligosaccharides and free FA were also determined. Overall, this work introduces a new bacterial member to the growing family of plant cell wall degrading FAEs that at present is largely of fungal origin, and it benchmarks the bioproduction of FA from triticale bran.
机译：从登革热厌氧杆菌的基因组中推定的\ u3b1 / \ u3b2水解酶折叠编码基因（基因标签TTE1809）被克隆并在大肠杆菌中表达，作为可能的热稳定阿魏酸酯酶（FAE）的来源，用于从生物质生产抗氧化剂酚酸。将33 kDa蛋白命名为TtFAE，纯化至表观同质性。 TtFAE的脂肪酶样序列特征及其对阿魏酸甲酯，芥子酸甲酯和对香豆酸甲酯的底物特异性将其分类为A型FAE的新成员。在75℃下，该酶至少保留其原始活性的95％超过80分钟；在80℃下，其半衰期为50分钟，这使TtFAE成为高度热稳定的蛋白质。在不同的水解条件下，从小黑麦麸制备的阿魏酸酯化低聚糖中释放出阿魏酸（FA）。在5小时的孵育时间内，黑小麦麸皮中总FA释放了30％，证明回收了68 mg FA / 100 g黑小麦麸皮。还确定了阿魏酸酯化低聚糖和游离FA的氧自由基吸收能力值。总体而言，这项工作为植物细胞壁降解FAEs的增长家族引入了新的细菌成员，而FAEs目前主要是真菌来源的，并且它是黑小麦麸皮生物生产的基准。

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