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Priestia megaterium
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY · 2023 · IF 5

Biosynthesis of resveratrol by an endophytic Priestia megaterium PH3 via the phenylpropane pathway

Zhang Xiaohan,Zhang Dong,Ding Yan,Li Zilong,Wang Chenchen,Ye Shuhong

Abstract Resveratrol (RES) is a secondary metabolite synthesized by plants in response to environmental stress and pathogen infection, which is of great significance for the industrial production of RES by fermentation culture. In this study, we aimed to explore the biosynthesis pathway of RES and its key enzymes in the Priestia megaterium PH3, which was isolated and screened from peanut fruit. Through Liquid Chromatography-Mass Spectrometry (LC-MS) analysis, we quantified the RES content and distribution in the culture medium and determined that Priestia megaterium PH3 mainly secreted RES extracellularly. Furthermore, the highest production of RES was observed in YPD, yielding an impressive 127.46 ± 6.11 μg/L. By optimizing the fermentation conditions, we achieved a remarkable RES yield of 946.82 ± 24.74 μg/L within just 2 days, which represents the highest reported yield for a natural isolate produced in such a short time frame. Our investigation revealed that the phenylpropane pathway is responsible for RES synthesis in this bacterium, with cinnamate 4-hydroxylase (C4H) identified as the main rate-limiting enzyme. Overall, our findings highlight the robust RES production capabilities of Priestia megaterium PH3, offering novel insights and potential applications for bacterial fermentation in RES production. Key points • RES synthesized by the bacterium was confirmed through the phenylpropane pathway. • The key rate-limiting enzyme for biosynthesis-RES is C4H. • RES reached 946.82 ± 24.74 μg/L after fermentation for 2 days. Graphical Abstract

CAS / MDL: 593-56-6 56-65-5
研究领域: 生物技术 · 微生物学 · 药学
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CURRENT MICROBIOLOGY · 2023 ·Vol. 80 ·期 9 ·1-9 · IF 2.6

Arginase from Priestia megaterium and the Effects of CMCS Conjugation on Its Enzymological Properties

Jiao Yu Liang,Shen Pin Quan,Wang Shu Fang,Chen Jing,Zhou Xiang Hong,Ma Gui Zhen

Arginase has shown promising potential in treating cancers by arginine deprivation therapy; however, low enzymatic activity and stability of arginase are impeding its development. This study was aimed to improve the enzymological properties of a marine bacterial arginase by carboxymethyl chitosan (CMCS) conjugation. An arginase producing marine bacterium Priestia megaterium strain P6 was isolated and identified. The novel arginase PMA from the strain was heterologously expressed, purified, and then conjugated to CMCS by ionic gelation with calcium chloride as the crosslinking agent. Enzymological properties of both PMA and CMCS-PMA conjugate were determined. The optimum temperature for PMA and CMCS-PMA at pH 7 were 60 °C and 55 °C, respectively. The optimum pH for PMA and CMCS-PMA at 37 °C were pH 10 and 9, respectively. CMCS-PMA showed higher thermostability than PMA over 55–70 °C and higher pH stability over pH 4–11 with the highest pH stability at pH 7. At 37 °C and pH of 7, i.e., around the human blood temperature and pH, CMCS-PMA was higher than the free PMA in enzymatic activity and stability by 24% and 21%, respectively. CMCS conjugation not only changed the optimum temperature, optimum pH, and enzymatic activity of PMA, but also improved its pH stability and temperature stability, and thus made it more favorable for medical application.

CAS / MDL: 10043-35-3 7558-79-4
研究领域: 生物化学 · 生物技术 · 药学 · 癌症研究
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Frontiers in Microbiology · 2025 · IF 4.5

Screening, identification, metabolic pathway of di-n-butyl phthalate degrading Priestia megaterium P-7 isolated from long-term film mulched cotton field soil in Xinjiang

Yuanyang Yi,Yuxian Wang,Wanqin Liu,Jing Zhu,Meiying Gu,Qiong Jia,Xue Li,Munire Mutalifu,Ling Jiang,Wei Zhang,Zhidong Zhang

Introduction: Di-n-butyl phthalate (DBP) is one of the most widely used phthalate esters (PAEs) and is considered an emerging global pollutant. It may pose a significant threat to ecosystem and human health due to its residual hazards and accumulation in the environment. Bacteria-driven PAE biodegradation is considered an economical and effective strategy for remediating such polluted environments.Methods: A DBP-degrading bacterium (P-7), was isolated from long-term film mulched cotton field soil. Its identity was confirmed via physiological, biochemical, and 16S rRNA gene analyses. The degradation conditions were optimized through single-factor experiments and response surface methodology (RSM).Furthermore, the whole-genome sequencing coupled with metabolomics was employed to elucidate metabolic mechanisms.Results: Priestia megaterium P-7 (P. megaterium P-7) achieved 100% DBP removal within 20 h under optimal conditions and exhibited broad substrate specificity for other PAEs. Genomic analysis identified key genes (lip, aes, ybfF, estA, and yvaK) encoding esterases/hydrolases that initiate DBP catabolism, converting it to phthalic acid (PA). Subsequent decarboxylation (pdc, bsdCD, mdcACDH, and lysA) and dioxygenase-mediated steps integrated PA into the TCA cycle. Metabolomics revealed three degradation pathways: decarboxylation (DBP → MBP → BB → BA→Catechol), hydrolysis (DBP → MBP → PA → PCA → Catechol) and direct β-oxidation (DBP → DEP → MEP → PA → Catechol).Conclusion: P. megaterium P-7 demonstrates exceptional degradation efficiency, substrate versatility, and environmental stress tolerance, making it a promising candidate for bioremediation of organic pollutants in contaminated soil.

研究领域: 微生物学 · 环境科学
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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES · 2025 · IF 8.5

Novel FAD-dependent uricase produced by food-sourced Priestia megaterium and activity assessment using hyperuricemia Caenorhabditis elegans

Haiyue Chen,Jun Xu,Han Shi,Xinle Liang,Wenjie Wang

The global rise in hyperuricemia (HUA) has driven the quest for safe, non-pharmacological interventions. Food-grade probiotics with HUA-mitigating potential are particularly promising. We isolated a novel strain, SSY-7-2, from traditional fermented wheat pastes, which exhibited robust uric acid (UA) degradation activity. SSY-7-2 showed high average nucleotide identity (ANI) values of 98.76–99.60 % with Priestia megaterium , surpassing the species delineation threshold. Whole-genome sequencing revealed complete UA degradation and purine metabolism pathways. We identified gene SSY_004365 as encoding an FAD-dependent urate hydroxylase (HpmO, E.C. 1.14.13.113), with a Km of 27.36 μM and a Kcat/Km of 5.74 × 10 4  s −1  M −1 . Using UA as the sole nitrogen source, we partially elucidated a conserved HpmO-UraD-HiuH cascade for UA hydrolysis in P. megaterium . Both in vitro and Caenorhabditis elegans models confirmed SSY-7-2's UA degradation activity, safety, and probiotic attributes. These findings expand the bioactivity spectrum of Priestia megaterium and position SSY-7-2 as a promising complementary probiotic for hyperuricemia management.

CAS / MDL: 146-14-5
研究领域: 微生物学 · 分子生物学 · 代谢疾病 · 营养科学 · 转化医学 · 药理学
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