Lu Yao, Jiang Qiang, Dong Yamin, Ji Runzhen, Xiao Yiwen, Zhu Du, Gao Boliang
Key Laboratory of Natural Microbial Medicine Research of Jiangxi Province, Jiangxi Science and Technology Normal University, Nanchang 330013, China.
Key Laboratory of Microbial Resources and Metabolism of Nanchang City, Jiangxi Science and Technology Normal University, Nanchang 330013, China.
BioTech (Basel). 2025 Mar 12;14(1):18. doi: 10.3390/biotech14010018.
The GH43 family of glycosidases represents an important class of industrial enzymes that are widely utilized across the food, pharmaceutical, and various other sectors. In this study, we identified a GH43 family glycoside hydrolytic enzyme, , derived from the plant endophytic fungus DX-THS3, which is capable of transforming several common ginsenosides. The enzyme function analysis reveals that Xyaf313 exhibits dual functionality, displaying both α-L-arabinofuranosidase and β-D-xylosidase activity. When acting as an α-L-arabinofuranosidase, Xyaf313 achieves optimal enzyme activity of 23.96 U/mg at a temperature of 50 °C and a pH of 7. In contrast, its β-D-xylosidase activity results in a slight reduction in enzyme activity to 23.24 U/mg, with similar optimal temperature and pH conditions to those observed for the α-L-arabinofuranosidase activity. Furthermore, Xyaf313 demonstrates considerable resistance to most metal ions and common chemical reagents. Notably, while the maximum enzyme activity of Xyaf313 occurs at 50 °C, it maintains high activity at room temperature (30 °C), with relative enzyme activity exceeding 90%. Measurements of ginsenoside transformation show that Xyaf313 can convert common ginsenosides Rc, Rb, Rb, and Rb into Rd, underscoring its potential for pharmaceutical applications. Overall, our findings contribute to the identification of a new class of bifunctional GH43 glycoside hydrolases, highlight the significance of plant endophytic fungi as a promising resource for the screening of carbohydrate-decomposing enzymes, and present new candidate enzymes for the biotransformation of ginsenosides.
糖苷水解酶的GH43家族是一类重要的工业酶，广泛应用于食品、制药和其他各个领域。在本研究中，我们从植物内生真菌DX-THS3中鉴定出一种GH43家族糖苷水解酶，它能够转化几种常见的人参皂苷。酶功能分析表明，Xyaf313具有双重功能，兼具α-L-阿拉伯呋喃糖苷酶和β-D-木糖苷酶活性。当作为α-L-阿拉伯呋喃糖苷酶时，Xyaf313在50℃和pH为7的条件下达到最佳酶活性23.96 U/mg。相比之下，其β-D-木糖苷酶活性导致酶活性略有降低，降至23.24 U/mg，最佳温度和pH条件与α-L-阿拉伯呋喃糖苷酶活性相似。此外，Xyaf313对大多数金属离子和常见化学试剂表现出相当的抗性。值得注意的是，虽然Xyaf313的最大酶活性出现在50℃，但它在室温（30℃）下仍保持高活性，相对酶活性超过90%。人参皂苷转化测量表明，Xyaf313可以将常见的人参皂苷Rc、Rb、Rb和Rb转化为Rd，突出了其在制药应用中的潜力。总体而言，我们的研究结果有助于鉴定一类新的双功能GH43糖苷水解酶，强调植物内生真菌作为筛选碳水化合物分解酶的有前途资源的重要性，并为人参皂苷的生物转化提供了新的候选酶。
