Biofilm formation on both biotic and abiotic surfaces accounts for a major factor in spread of antimicrobial resistance. Due to their ubiquitous nature, biofilms are of great concern for environment as well as human health. In the present study, an integrated process for the co-production of a cocktail of carbohydrases from a natural variant of Aspergillus niger was designed. The enzyme cocktail was found to have a noteworthy potential to eradicate/disperse the biofilms of selected pathogens. For application of enzymes as an antibiofilm agent, the enzyme productivities were enhanced by statistical modelling using response surface methodology (RSM). The antibiofilm potential of the enzyme cocktail was studied in terms of (i) in vitro cell dispersal assay (ii) release of reducing sugars from the biofilm polysaccharides (iii) the effect of enzyme treatment on biofilm cells and architecture by confocal laser scanning microscopy (CLSM). Potential of the enzyme cocktail to disrupt/disperse the biofilm of selected pathogens from biopolymer surfaces was also assessed by field emission scanning electron microscopy (FESEM) analysis. Further, their usage in conjunction with antibiotics was assessed and it was inferred from the results that the use of enzyme cocktail augmented the efficacy of the antibiotics. The study thus provides promising insights into the prospect of using multiple carbohydrases for management of heterogeneous biofilms formed in natural and clinical settings.
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http://dx.doi.org/10.1186/s13568-021-01183-y | DOI Listing |
Sci Rep
January 2025
BBF, Biodiversité et Biotechnologie Fongiques, INRAE, Aix-Marseille Univ, Marseille, France.
Int J Biol Macromol
January 2025
Forest Product Biotechnology/Bioenergy Group, Department of Wood Science, University of British Columbia, 2424 Main Mal, Vancouver V6T 1Z4, Canada. Electronic address:
Modern enzyme cocktails often include lytic polysaccharide monooxygenase (LPMO) as an accessory enzyme that enhances cellulose accessibility during hydrolysis. Although lignin is known to generally impede cellulose hydrolysis, previous research has demonstrated lignin's potential to act as a co-factor in boosting LPMO activity and that the negative impact of lignin limiting enzyme accessibility can be mitigated by sulfonated. When sulphonated lignin was added to microcrystalline cellulose (Avicel) the activity of the lytic polysaccharide monooxygenase (LPMO) was boosted, as determined when using a quartz crystal microbalance and dissipation monitoring (QCM-D).
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
College of Forestry, Henan Agricultural University, Zhengzhou 450046, China. Electronic address:
In this study, we fully sequenced and analyzed the genome of strain 12219 and identified it as Streptomyces thermocarboxydus. The genome contained a single linear chromosome, 6,950,031 bp in size, with a GC content of 72.21 %.
View Article and Find Full Text PDFLancet Microbe
December 2024
Institute of Infectious Diseases and Tropical Medicine, LMU University Hospital, LMU Munich, Germany; German Center for Infection Research, Munich Partner Site, Munich, Germany; Fraunhofer Institute for Translational Medicine and Pharmacology ITMP, Immunology, Infection, and Pandemic Research, Munich, Germany; Unit Global Health, Helmholtz Zentrum München, German Research Center for Environmental Health, Neuherberg, Germany. Electronic address:
Background: The broad use of bedaquiline and pretomanid as the mainstay of new regimens to combat tuberculosis is a risk due to increasing bedaquiline resistance. We aimed to assess the safety, bactericidal activity, and pharmacokinetics of BTZ-043, a first-in-class DprE1 inhibitor with strong bactericidal activity in murine models.
Methods: This open-label, dose-expansion, randomised, controlled, phase 1b/2a trial was conducted in two specialised tuberculosis sites in Cape Town, South Africa.
Clin Pharmacol Ther
January 2025
Drug Clinical Trial Center, Peking University Third Hospital, Beijing, China.
OATP1B, P-gp, BCRP, and CYP3A are the most contributing drug-metabolizing enzymes or transporters (DMETs) for commonly prescribed medication. Their activities may change in end-stage renal disease (ESRD) patients with large inter-individual variabilities (IIVs), leading to altered substrate drug exposure and ultimately elevated safety risk. However, the changing extent and indictive influencing factors are not quantified so far.
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