Hunan Province Key Laboratory of Plant Functional Genomics and Developmental Regulation, College of Biology, Hunan University, Changsha, Hunan, 410008, People's Republic of China.
Central South University of Forestry and Technology, Changsha, 410004, Hunan, People's Republic of China.
Biotechnol Lett. 2020 Aug;42(8):1479-1488. doi: 10.1007/s10529-020-02855-8. Epub 2020 Mar 6.
Identification and characterization of a novel bacterial carbohydrate esterase (PaCes7) with application potential for lignocellulose and pesticide degradation.
PaCes7 was identified from the lignocellulolytic bacterium, Pantoea ananatis Sd-1 as a new carbohydrate esterase. Recombinant PaCes7 heterologously expressed in Escherichia coli showed a clear preference for esters with short-chain fatty acids and exhibited maximum activity towards α-naphthol acetate at 37 °C and pH 7.5. Purified PaCes7 exhibited its catalytic activity under mesophilic conditions and retained more than 40% activity below 30 °C. It displayed a relatively wide pH stability from pH 6-11. Furthermore, the enzyme was strongly resistant to Mg, Pb, and Co and activated by K and Ca. Both P. ananatis Sd-1 and PaCes7 could degrade the pesticide carbaryl. Additionally, PaCes7 was shown to work in combination with cellulase and/or xylanase in rice straw degradation.
The data suggest that PaCes7 possesses promising biotechnological potential.
鉴定和表征一种新型细菌碳水化合物酯酶（PaCes7），该酶具有用于木质纤维素和农药降解的应用潜力。
从木质纤维素降解菌 Pantoea ananatis Sd-1 中鉴定出 PaCes7 是一种新型碳水化合物酯酶。在大肠杆菌中异源表达的重组 PaCes7 对短链脂肪酸酯表现出明显的偏好，并在 37°C 和 pH7.5 下对 α-萘酚乙酸酯表现出最大活性。纯化的 PaCes7 在嗜温条件下表现出其催化活性，并在低于 30°C 时保留超过 40%的活性。它在 pH6-11 之间表现出相对较宽的 pH 稳定性。此外，该酶对 Mg、Pb 和 Co 具有很强的抗性，并被 K 和 Ca 激活。P. ananatis Sd-1 和 PaCes7 均可降解农药西维因。此外，研究表明 PaCes7 可与纤维素酶和/或木聚糖酶协同作用降解水稻秸秆。
数据表明 PaCes7 具有有前途的生物技术潜力。
