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Feruloyl esterase (FAE-1) sourced from a termite hindgut and GH10 xylanases synergy improves degradation of arabinoxylan
AMB Express ( IF 3.5 ) Pub Date : 2021-01-19 , DOI: 10.1186/s13568-021-01180-1
Mpho S. Mafa , Samkelo Malgas , Brett I. Pletschke

Cereal feedstocks have high arabinoxylan content as their main hemicellulose, which is linked to lignin by hydroxycinnamic acids such as ferulic acid. The ferulic acid is linked to arabinoxylan by ester bonds, and generally, the high substitution of ferulic acid leads to a loss of activity of xylanases targeting the arabinoxylan. In the current study, a feruloyl esterase (FAE-1) from a termite hindgut bacteria was functionally characterised and used in synergy with xylanases during xylan hydrolysis. The FAE-1 displayed temperature and pH optima of 60 ℃ and 7.0, respectively. FAE-1 did not release reducing sugars from beechwood xylan (BWX), wheat arabinoxylan (WAX) and oat spelt xylan (OX), however, displayed high activity of 164.74 U/mg protein on p-nitrophenyl-acetate (pNPA). In contrast, the GH10 xylanases; Xyn10 and XT6, and a GH11 xylanase, Xyn2A, showed more than two-fold increased activity on xylan substrates with low sidechain substitutions; BWX and OX, compared to the highly branched substrate, WAX. Interestingly, the FAE-1 and GH10 xylanases (Xyn10D and XT6) displayed a degree of synergy (DS) that was higher than 1 in all enzyme loading combinations during WAX hydrolysis. The 75%XT6:25%FAE-1 synergistic enzyme combination increased the release of reducing sugars by 1.34-fold from WAX compared to the control, while 25%Xyn10D:75%FAE-1 synergistic combination released about 2.1-fold of reducing sugars from WAX compared to controls. These findings suggest that FAE-1 can be used in concert with xylanases, particularly those from GH10, to efficiently degrade arabinoxylans contained in cereal feedstocks for various industrial settings such as in animal feeds and baking.



中文翻译:

源自白蚁后肠的阿魏酸酯酶(FAE-1)和GH10木聚糖酶的协同作用可改善阿拉伯木聚糖的降解

谷物原料具有较高的阿拉伯木聚糖含量作为其主要半纤维素,其通过羟基肉桂酸(例如阿魏酸)与木质素连接。阿魏酸通过酯键与阿拉伯木聚糖连接,并且通常,阿魏酸的高取代导致靶向阿拉伯木聚糖的木聚糖酶的活性丧失。在当前的研究中,功能上表征了白蚁后肠细菌的阿魏酸酯酶(FAE-1),并在木聚糖水解过程中与木聚糖酶协同作用。FAE-1的最佳温度和pH分别为60℃和7.0。FAE-1不会从山毛榉木聚糖(BWX),小麦阿拉伯木聚糖(WAX)和燕麦拼写木聚糖(OX)中释放还原糖,但是在p上表现出164.74 U / mg蛋白的高活性乙酸硝基苯酯(pNPA)。相反,GH10木聚糖酶;Xyn10和XT6以及GH11木聚糖酶Xyn2A在具有低侧链取代的木聚糖底物上显示出超过两倍的活性增加;与高度支化的底物WAX相比,BWX和OX。有趣的是,在WAX水解过程中,在所有酶负载组合中,FAE-1和GH10木聚糖酶(Xyn10D和XT6)的协同作用(DS)都高于1。与对照相比,75%XT6:25%FAE-1协同酶组合从WAX释放的还原糖增加了1.34倍,而25%Xyn10D:75%FAE-1协同组合释放了约2.1倍的还原糖。 WAX与控件相比。这些发现表明,FAE-1可与木聚糖酶(尤其是GH10的木聚糖酶)一起使用,

更新日期:2021-01-19
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