Characterization of a highly thermostable recombinant xylanase from Anoxybacillus ayderensis

IF 1.4 4区生物学 Q4 BIOCHEMICAL RESEARCH METHODS

Protein expression and purification Pub Date : 2024-04-01 DOI:10.1016/j.pep.2024.106478

Zuleyha Akpinar , Hakan Karaoglu

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引用次数: 0

Abstract

Xylanases are the main enzymes to hydrolyze xylan, the major hemicellulose found in lignocellulose. Xylanases also have a wide range of industrial applications. Therefore, the discovery of new xylanases has the potential to enhance efficiency and sustainability in many industries. Here, we report a xylanase with thermophilic character and superior biochemical properties for industrial use. The new xylanase is discovered in Anoxybacillus ayderensis as an intracellular xylanase (AAyXYN329) and recombinantly produced. While AAyXYN329 shows significant activity over a wide pH and temperature range, optimum activity conditions were determined as pH 6.5 and 65 °C. The half-life of the enzyme was calculated as 72 h at 65 °C. The enzyme did not lose activity between pH 6.0–9.0 at +4 °C for 75 days. Km, kcat and kcat/Km values of AAyXYN329 were calculated as 4.09824 ± 0.2245 μg/μL, 96.75 1/sec, and 23.61/L/g.s ⁻¹, respectively. In conclusion, the xylanase of A. ayderensis has an excellent potential to be utilized in many industrial processes.

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来自 Anoxybacillus ayderensis 的高热稳定性重组木聚糖酶的表征

木聚糖酶是水解木聚糖的主要酶，木聚糖是木质纤维素中的主要半纤维素。木聚糖酶还具有广泛的工业用途。因此，发现新的木聚糖酶有可能提高许多行业的效率和可持续性。在此，我们报告了一种具有嗜热特性和优异生化性能的木聚糖酶，可用于工业用途。这种新型木聚糖酶是在 Anoxybacillus ayderensis 中发现并重组生产的一种胞内木聚糖酶（AAyXYN329）。AAyXYN329 在很宽的 pH 值和温度范围内都显示出显著的活性，最佳活性条件被确定为 pH 值 6.5 和 65 °C。在 65 ℃ 下，酶的半衰期为 72 小时。在 +4 °C、pH 值为 6.0-9.0 的条件下，该酶 75 天内都没有失去活性。经计算，AAyXYN329 的 Km、kcat 和 kcat/Km 值分别为 4.09824 ± 0.2245 μg/μL、96.75 1/sec 和 23.61/L/g.s-1。总之，A. ayderensis 的木聚糖酶具有在许多工业过程中加以利用的巨大潜力。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Protein expression and purification 生物-生化研究方法

CiteScore

3.70

自引率

6.20%

发文量

120

审稿时长

32 days

期刊介绍： Protein Expression and Purification is an international journal providing a forum for the dissemination of new information on protein expression, extraction, purification, characterization, and/or applications using conventional biochemical and/or modern molecular biological approaches and methods, which are of broad interest to the field. The journal does not typically publish repetitive examples of protein expression and purification involving standard, well-established, methods. However, exceptions might include studies on important and/or difficult to express and/or purify proteins and/or studies that include extensive protein characterization, which provide new, previously unpublished information.