The increasing number of resistant bacterial strains has raised efforts in developing alternative treatment strategies. Lipase is highly expressed in most bacteria and lipase targeting dyes will be non-sacrificed materials for a sustainable method against microorganism. The combination of chemotherapy and antimicrobial photodynamic inactivation (aPDI) method will be an effective method due to enhanced antibacterial activity. Here we reported the spectroscopic features of five boron dipyrrolylmethene (BODIPY) derivatives with different functional groups for lipase affinity and antibacterial activity. Lipase affinity tests and antibacterial assays were conducted by spectroscopic methods. Adamantane-conjugated BODIPY (BDP-2) was found to be the active compound against E. coli. Next, BDP-2 was brominated, and then assembled with PEG resulting biocompatible BDP2-Br@mPEG nanoparticles. The MTT assay indicated that BDP2-Br@mPEG was less toxicity on BGC-823 cancer cells without irradiation. The BDP2-Br@mPEG can inhibit the proliferation of E. coli and damage the membrane of bacterial cell under green LED light irradiation. The results proved BDP2-Br@mPEG can be a very promising green LED light driven antibacterial material.
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http://dx.doi.org/10.1016/j.saa.2020.118252 | DOI Listing |
Crit Rev Food Sci Nutr
January 2025
Shandong Provincial Innovation Center for Dairy Technology, Zibo, P.R. China.
The dairy industry is progressively integrating advanced enzyme technologies to optimize processing efficiency and elevate product quality. Among these technologies, enzyme immobilization has emerged as a pivotal innovation, offering considerable benefits in terms of enzyme reusability, stability, and overall process sustainability. This review paper explores the latest improvements in enzyme immobilization techniques and their industrial applications within milk processing.
View Article and Find Full Text PDFAppl Biochem Biotechnol
January 2025
Department of Food Engineering, State University of Maringá, Maringá, PR, Brazil.
Lipases have catalytic capacity in various processes such as hydrolysis. Those derived from plant sources, such as linseed, offer an economical alternative. The immobilization process facilitates the recovery and reuse of lipase, providing advantages such as resistance to high temperatures and difficulties in recovering and reusing free lipases, which makes product separation difficult.
View Article and Find Full Text PDFEur J Med Chem
January 2025
Department of Radiology and Imaging Sciences, Emory University, 1364 Clifton Road, Atlanta, GA, 30322, United States. Electronic address:
Monoacylglycerol lipase (MAGL) is a 33 kDa cytosolic serine hydrolase that is widely distributed in the central nervous system and peripheral tissues. MAGL hydrolyzes monoacylglycerols into fatty acids and glycerol, playing a crucial role in endocannabinoid degradation. Inhibition of MAGL in the brain elevates levels of 2-arachidonoylglycerol and leads to decreased pro-inflammatory prostaglandin and thromboxane production.
View Article and Find Full Text PDFAppl Biochem Biotechnol
January 2025
Department of Life Science and Biochemical Engineering, Graduate School, SunMoon University, Asan, 31460, Republic of Korea.
Antarctic organisms are known for producing unique secondary metabolites, and this study specifically focuses on the less-explored metabolites of the moss Warnstorfia fontinaliopsis. To evaluate their potential bioactivity, we extracted secondary metabolites using four different solvents and identified significant lipase inhibitory activity in the methanol extract. Non-targeted metabolomic analysis using liquid chromatography-tandem mass spectrometry (LC-MS/MS) on this extract predicted the presence of 12 compounds, including several not previously reported in mosses.
View Article and Find Full Text PDFEur J Med Chem
February 2025
LEPABE-Laboratory for Process Engineering, Environment, Biotechnology and Energy, Faculty of Engineering, University of Porto, Rua Dr. Roberto Frias, s/n, 4200-465, Porto, Portugal; ALICE-Associate Laboratory for Innovation in Chemical Engineering, Faculty of Engineering, University of Porto, Rua Dr. Roberto Frias, s/n, 4200-465, Porto, Portugal; DEQ-Department of Chemical Engineering, Faculty of Engineering, University of Porto, Rua Dr. Roberto Frias, s/n, 4200-465, Porto, Portugal. Electronic address:
Iron is essential for the formation, maturation and dispersal of bacterial biofilms, playing a crucial role in the physiological and metabolic functions of bacteria as well as in the regulation of virulence. Limited availability of iron can impair the formation of robust biofilms by altering cellular motility, hydrophobicity and protein composition of the bacterial surface. In this study, the antibiofilm activity of two natural iron chelating agents, kojic acid (5-hydroxy-2-hydroxymethyl-4H-pyran-4-one) and maltol (3-hydroxy-2-methyl-4-pyrone), were investigated against Staphylococcus aureus and Pseudomonas aeruginosa.
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