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Arabinoxylo- and Arabino-Oligosaccharides-Specific α-L-Arabinofuranosidase GH51 Isozymes from the Amylolytic Yeast Saccharomycopsis fibuligera.
Journal of Microbiology and Biotechnology ( IF 2.5 ) Pub Date : 2021-01-01 , DOI: 10.4014/jmb.2012.12038
Tae Hyeon Park 1 , Chang-Yun Choi 1 , Hyeon Jin Kim 2 , Jeong-Rok Song 1 , Damee Park 1 , Hyun Ah Kang 2 , Tae-Jip Kim 1
Affiliation  

Two genes encoding the probable α-L-arabinofuranosidase (EC 3.2.1.55) isozymes with 92.3% amino acid sequence identity, ABF51A and ABF51B, were found from the chromosomes 3 and 5 of Saccharomycopsis fibuligera KJJ81, the amylolytic yeast isolated from Korean wheat-based Nuruk, respectively. Each open reading frame consists of 1,551 nucleotides which encodes a protein of 517 amino acids with the molecular mass of approximately 59 kDa. These isozymes share approximately 49% of amino acid sequence identities with eukaryotic ABFs from the filamentous fungi. The corresponding genes were cloned, functionally expressed, and purified from Escherichia coli. SfABF51A and SfABF51B showed the highest activities on p-nitrophenyl arabinofuranoside at 40~45°C and pH 7.0 in sodium phosphate buffer and at 50°C and pH 6.0 in sodium acetate buffer, respectively. These exo-acting enzymes belonging to the Glycoside Hydrolase (GH) family 51 could hydrolyze arabinoxylo-oligosaccharides (AXOS) and arabino-oligosaccharides (AOS) to produce only L-arabinose, whereas they could hardly degrade any polymeric substrates including arabinans and arabinoxylans. The detailed product analyses revealed that both SfABF51 isozymes can catalyze the versatile hydrolysis of α-(1,2)- and α-(1,3)-L-arabino furanosidic linkages of AXOS, and α-(1,2)-, α-(1,3)-, and α-(1,5)-linkages of linear and branched AOS. On the contrary, they have much lower activity against the α-(1,2)- and α-(1,3)-double substituted substrates than the single substituted ones. These hydrolases are supposed to play the important roles in the degradation and utilization of hemicellulosic biomass by S. fibuligera.

中文翻译:

来自淀粉分解酵母 Saccharomycopsis fibuligera 的阿拉伯木糖和阿拉伯寡糖特异性 α-L-阿拉伯呋喃糖苷酶 GH51 同工酶。

从Saccharomycopsis fibuligera KJJ81的染色体 3 和 5 中发现了两个编码可能具有 92.3% 氨基酸序列同一性的 α-L-阿拉伯呋喃糖苷酶 (EC 3.2.1.55) 同工酶的基因ABF51AABF51B ,这是从韩国小麦中分离的淀粉分解酵母基于努鲁克,分别。每个开放阅读框由 1,551 个核苷酸组成,编码 517 个氨基酸的蛋白质,分子量约为 59 kDa。这些同工酶与来自丝状真菌的真核 ABF 共享大约 49% 的氨基酸序列同一性。从大肠杆菌中克隆、功能表达和纯化相应的基因。SfABF51 A和 SfABF51 B在 40~45°C 和 pH 7.0 的磷酸钠缓冲液中以及在 50°C 和 pH 6.0 的乙酸钠缓冲液中分别显示出对硝基苯阿拉伯呋喃糖苷最高活性。这些exo属于糖苷水解酶 (GH) 家族 51 的作用酶可以水解阿拉伯木寡糖 (AXOS) 和阿拉伯寡糖 (AOS) 以仅产生 L-阿拉伯糖,而它们几乎不能降解任何聚合物底物,包括阿拉伯聚糖和阿拉伯木聚糖。详细的产物分析表明,两种 SfABF51 同工酶都可以催化 AXOS 的 α-(1,2)- 和 α-(1,3)-L-阿拉伯呋喃糖苷键以及 α-(1,2)-,线性和支化 AOS 的 α-(1,3)- 和 α-(1,5)- 连接。相反,它们对 α-(1,2)- 和 α-(1,3)- 双取代底物的活性远低于单取代底物。这些水解酶被认为在S. fibuligera降解和利用半纤维素生物质中发挥重要作用。
更新日期:2021-01-07
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