枯草芽孢杆菌
磷脂酰丝氨酸
分泌物
磷脂酰胆碱
酶
信号肽
磷脂酶D
磷脂酶A2
化学
磷脂酶
生物化学
产量(工程)
水溶液
生物
磷脂
重组DNA
有机化学
细菌
基因
材料科学
遗传学
膜
冶金
作者
Shuhong Mao,Zhaohui Zhang,Xiaoyu Ma,Huan Tian,Fuping Lu,Yihan Liu
标识
DOI:10.1016/j.ijbiomac.2020.12.103
摘要
Transphosphatidylation catalyzed by phospholipase D has gained increasing attention for producing phosphatidylserine (PS), which can be used in functional food and medicine. In this study, we investigated the effects of six signal peptides on the secretion of PLD (PLDsa) from Streptomyces antibioticus TCCC 21059 in the food-grade GRAS bacterium Bacillus subtilis. It indicated that the optimal signal peptide DacB with an Ala-X-Ala sequence motif at the C-terminus showed the highest secretory expression ability, resulting in increased production of 2.84 U/mL PLDsa. Then PLDsa was immobilized on the epoxy-based carriers, and one of these carriers allowed PLDsa loading of up to 2.7 mg/g. The immobilized PLDsa was more stable over a wide range of pH value (4.5–7.5) and temperature (16 °C–60 °C) than free PLDsa. Subsequently, the synthesis of PS from soybean phosphatidylcholine (PC) was carried out in purely aqueous solution using immobilized PLDsa, leading to a high yield of 65%. The immobilized PLDsa catalyst maintained a relative PS production of 60% after 5 recycles. Notably, the use of toxic solvent was completely eliminated in the whole process, which would be more profitable for the application of PS.
科研通智能强力驱动
Strongly Powered by AbleSci AI