Molecular cloning and characterization of a novel xylanase from Microbacterium imperiale YD-01,Journal of Food Biochemistry

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Molecular cloning and characterization of a novel xylanase from Microbacterium imperiale YD-01
Journal of Food Biochemistry ( IF 3.5 ) Pub Date : 2021-11-03 , DOI: 10.1111/jfbc.13988
Keqin Tang _{1,

2} , Yin Cui ₂ , Jingyi Xiao ₃ , Mengyao Ding ₂ , Hongjun Chao ₂ , Jing Wu ₂ , Zhenggang Han ₂ , Jun Liu ₂ , Xin Li ₂ , Dazhong Yan _{1,

2}

Affiliation

Xylaneses are very common xylanolytic enzymes, which are widely used in food, papermaking, and other industries. In this study, a xylanase-encoding gene xyn1923, which encodes a protein of 1352 amino acids, was identified through the whole genome analysis of Microbacterium imperiale YD-01. Bioinformatics analysis showed that Xyn1923 only had maximum similarity of 37% with the reported xylanase from Alkalihalobacillus halodurans C-125, indicating that Xyn1923 was a novel xylanase. The enzymatic properties of Xyn1923 were systematically analyzed after purification. The results showed that the specific activity of the enzyme was 10.582 ± 0.413 U/mg, while the optimum pH and temperature of the enzyme were 7.0 and 70°C, respectively. The enzyme is stable in the pH range of 6.0–9.0, and the enzyme activity could maintain more than 85% of the original activity after 16 hr incubation at pH 9.0. The enzyme activity is relatively stable in the range of 30–60°C, and its enzyme activity could maintain more than 89% of the original activity after treatment at 60°C for 30 min. Low concentrations (≤1 mM) of Co²⁺, Ba²⁺, Fe²⁺, and Fe³⁺ metal ions exerted a stimulatory effect on the activity of Xyn1923. And in contrast, high concentrations (≥2 mM) of the above metal ions inhibit the activity of Xyn1923. Mg²⁺, Ag⁺, Cu²⁺, Ca²⁺, Mn²⁺, and Pb²⁺ ions showed a negative effect on the activity of Xyn1923. Enzyme kinetic studies showed that K_m and V_max values for xylan were 7.842 ± 0.538 mg/ml and 15.208 ± 0.822 U/mg, respectively. Xyn1923 was found to be a weakly alkaline thermophilic xylanase through an enzymatic property analysis.

中文翻译：

一种来自帝王微杆菌 YD-01 的新型木聚糖酶的分子克隆和表征

木聚糖酶是非常常见的木聚糖分解酶，广泛应用于食品、造纸等行业。本研究通过对Microbacterium Imperiale YD-01的全基因组分析，鉴定出一个编码1352个氨基酸的蛋白质的木聚糖酶编码基因xyn1923 。生物信息学分析表明，Xyn1923 与已报道的来自嗜盐碱盐杆菌的木聚糖酶的最大相似性仅为 37% 。C-125，表明Xyn1923是一种新型木聚糖酶。纯化后对Xyn1923的酶学性质进行了系统分析。结果表明，酶的比活性为10.582±0.413 U/mg，酶的最适pH和温度分别为7.0和70℃。该酶在pH 6.0-9.0范围内稳定，在pH 9.0孵育16小时后，酶活性可维持在原活性的85%以上。酶活力在30~60℃范围内较为稳定，60℃处理30 min后酶活力可维持在原有活力的89%以上。低浓度 (≤1 mM) Co ²⁺、Ba ²⁺、Fe ²⁺和 Fe ³⁺金属离子对 Xyn1923 的活性有刺激作用。相比之下，高浓度（≥2 mM）的上述金属离子会抑制 Xyn1923 的活性。Mg ²⁺、Ag ⁺、Cu ²⁺、Ca ²⁺、Mn ²⁺和Pb ²⁺离子对Xyn1923的活性有负面影响。酶动力学研究表明，木聚糖的K _m和V_最大值分别为 7.842 ± 0.538 mg/ml 和 15.208 ± 0.822 U/mg。通过酶学性质分析发现 Xyn1923 是一种弱碱性嗜热木聚糖酶。

更新日期：2021-12-09

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