The extracellular Aspergillus niger GZUF36 lipase (EXANL1) has broad applicability such as synthesis of functional lipids. The wild-type strain is unstable, and the culture time is long. Studies on the selectivity of substrates for EXANL1 are not available. Therefore, this study aimed to express, purify, characterize and analyze the substrate specificity of EAXNL1. The results showed that EXANL1 was stable in the presence of 40 % (v/v) dimethyl sulfoxide, glycerol, toluene, and n-hexane. The relative activity was 104 %, 88 %, 81 %, and 76 %. The residual enzyme activity of EXANL1 was more than 85 % in surfactants with a low concentration. EXANL1 exhibited a high conversion rate (79 %) for p-nitrophenyl palmitate. The molecular docking of p-nitrophenyl palmitate into the active site of EXANL1 indicated that the preference for this fatty acid chain length might be due to the formation of hydrogen bonds. The distance between the carbonyl carbon atom of p-nitrophenyl palmitate and the nucleophilic oxygen atom of serine 162 was 2.91 Å. Both experiments revealed that EXANL1 exhibited higher specificity for p-nitrophenyl palmitate. These results indicated that EXANL1 could be a promising tool in organic synthesis and detergent industry. The molecular docking provided a basis for the explanation on the substrate selectivity of EXANL1.

细胞外黑曲霉GZUF36 脂肪酶 (EXANL1) 具有广泛的适用性，如功能性脂质的合成。野生型菌株不稳定，培养时间长。没有关于底物对 EXANL1 的选择性的研究。因此，本研究旨在表达、纯化、表征和分析 EAXNL1 的底物特异性。结果表明，EXANL1 在 40% ( v/v ) 二甲基亚砜、甘油、甲苯和正己烷存在下是稳定的。相对活性为 104 %、88 %、81 % 和 76 %。EXANL1在低浓度表面活性剂中的残留酶活性超过85%。EXANL1 对对硝基苯基棕榈酸酯表现出高转化率 (79%) 。p的分子对接-硝基苯基棕榈酸酯进入 EXANL1 的活性位点表明对这种脂肪酸链长度的偏好可能是由于形成了氢键。对硝基苯基棕榈酸酯的羰基碳原子与丝氨酸 162 的亲核氧原子之间的距离为 2.91 Å。两个实验都表明 EXANL1 对对硝基苯基棕榈酸酯表现出更高的特异性。这些结果表明 EXANL1 可能是有机合成和洗涤剂工业中很有前途的工具。分子对接为解释EXANL1的底物选择性提供了基础。