Estrogen contamination is widespread and microbial degradation is a promising removal method; however, unfavorable environments can hinder microbial function. In this study, a natural estrogen 17-estradiol (E2) was introduced as a degradation target, and a new combination of bacterial carrier was investigated. We found the best combination of polyvinyl alcohol (PVA) and sodium alginate (SA) was 4% total concentration, PVA:SA = 5:5, with nano-FeO at 2%, and maltose and glycine added to promote degradation, for which the optimal concentrations were 5 g·L and 10 g·L, respectively. Based on the above exploration, the bacterial carrier was made, and the degradation efficiency of the immobilized bacteria reached 92.3% in 5 days. The immobilized bacteria were reused for three cycles, and the degradation efficiency of each round could exceed 94%. Immobilization showed advantages at pH 5, pH 11, 10 °C, 40 °C, and 40 g·L NaCl, and the degradation efficiency of the immobilized bacteria was higher than 90%. In the wastewater, the immobilized bacteria could degrade E2 to about 1 mg·L on the 5th day. This study constructed a bacterial immobilization carrier using a new combination, explored the application potential of the carrier, and provided a new choice of bacterial immobilization carrier.
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http://dx.doi.org/10.3390/molecules27185807 | DOI Listing |
BMC Microbiol
January 2025
Department of Neurology, Yongchuan Hospital of Chongqing Medical University, Chongqing, China.
Background: Depression is a common mental disorder accompanied by gut microbiota dysbiosis, which disturbs the metabolism of the host. While diurnal oscillation of the intestinal microbiota is involved in regulating host metabolism, the characteristics of the intestinal microbial circadian rhythm in depression remain unknown. Our aim was to investigate the microbial circadian oscillation signature and related metabolic pathways in a mouse model with depression-like behaviours.
View Article and Find Full Text PDFProtein Sci
February 2025
Center for Cooperative Research in Biomaterials (CIC biomaGUNE), Basque Research and Technology Alliance (BRTA), San Sebastián, Spain.
Enzyme immobilization is indispensable for enhancing enzyme performance in various industrial applications. Typically, enzymes require specific spatial arrangements for optimal functionality, underscoring the importance of correct orientation. Despite well-known N- or C-terminus tailoring techniques, alternatives for achieving orientation control are limited.
View Article and Find Full Text PDFChembiochem
January 2025
Chinese Academy of Medical Sciences & Peking Union Medical College Institute of Materia Medica, State Key Laboratory of Bioactive Substances and Function of Natural Medicine, 1 Xian Nong Tan Street, 100050, Beijing, CHINA.
Bacterial infections, particularly those caused by drug-resistant bacteria, represent a pressing global health challenge. During the interaction between pathogen infection and host defense, bacterial infections initiate the host's immune response, which involves the activation of proteases that play a critical role in antibacterial defense. Granzyme B (GzmB), a key immune-related biomarker associated with cytotoxic T lymphocytes (CTLs), plays a pivotal role in this process.
View Article and Find Full Text PDFSci Rep
January 2025
Faculty of Allied Health Sciences, Center of Excellence for Innovative Diagnosis of Antimicrobial Resistance, Chulalongkorn University, Bangkok, 10330, Thailand.
Rifampicin-resistant tuberculosis (RR-TB) is a critical issue with significant implications for patient care, public health, and TB control efforts that necessitate comprehensive strategies for detection. This study presents a novel point-of-care diagnostic tool for RR-TB detection employing a peptide nucleic acid (PNA)-paper-based sensor combined with isothermal recombinase polymerase amplification (RPA). The sensor targets mutations in codons 516, 526, and 531 of the rpoB gene, the top three common mutations associated with rifampicin-resistant strains.
View Article and Find Full Text PDFAppl Microbiol Biotechnol
January 2025
Department of Chemistry, Biochemistry and Pharmaceutical Sciences, University of Bern, Freiestrasse 3, 3012, Bern, Switzerland.
A new strategy has been developed to successfully produce the active component danshensu ex vivo. For this purpose, phenylalanine dehydrogenase from Bacillus sphaericus was combined with the novel hydroxyphenylpyruvate reductase from Mentha x piperita, thereby providing an in situ cofactor regeneration throughout the conversion process. The purified enzymes were co-immobilized and subsequently employed in batch biotransformation, resulting in 60% conversion of 10 mM L-dopa within 24 h, with a catalytic amount of NAD as cofactor.
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