Serratiopeptidase, a proteolytic enzyme serves as an important anti-inflammatory and analgesic medication. Present study reports the production and purification of extracellular serratiopeptidase from an endophyte, MES-4, isolated from . Purification of the enzyme by Ion exchange chromatography led to the specific activity of 13,030 U/mg protein of serratiopeptidase, showcasing about 3.1 fold enhanced activity. The catalytic domain of the purified serratiopeptidase, composed of Zn coordinated with three histidine residues (His 209, His 213, and His 219), along with glutamate (Glu 210) and tyrosine (Tyr 249). The molecular mass, as determined by SDS-PAGE was ∼51 kDa. The purified serratiopeptidase displayed optimal activity at pH 9.0, temperature 50°C. Kinetic studies revealed V and K values of 33,333 U/mL and 1.66 mg/mL, respectively. Further, optimized conditions for the production of serratiopeptidase by Taguchi design led to the productivity of 87 U/mL/h with 87.9 fold enhanced production as compared to the previous conditions.

中文翻译：

---

粘质沙雷菌 MES-4 中沙雷肽酶的纯化、功能表征和增强生产：从桑树中分离出的内生菌

沙雷肽酶是一种蛋白水解酶，是一种重要的抗炎和镇痛药物。目前的研究报告了从分离自 的内生菌 MES-4 中生产和纯化胞外锯齿肽酶。通过离子交换色谱法纯化该酶，得到舍拉肽酶的比活性为 13,030 U/mg 蛋白质，显示出约 3.1 倍的增强活性。纯化的锯齿肽酶的催化结构域由与三个组氨酸残基（His 209、His 213 和 His 219）以及谷氨酸（Glu 210）和酪氨酸（Tyr 249）配位的 Zn 组成。通过 SDS-PAGE 测定，分子量为 ∼51 kDa。纯化的锯齿肽酶在 pH 9.0、温度 50°C 时表现出最佳活性。动力学研究显示 V 和 K 值分别为 33,333 U/mL 和 1.66 mg/mL。此外，通过田口设计优化了沙雷肽酶的生产条件，生产率达到 87 U/mL/h，与之前的条件相比，产量提高了 87.9 倍。