Researchers are consistently investigating novel and distinctive methods and materials that are compatible for human life and environmental conditions This study aimed to synthesize gold nanoparticles (ALPs-AuNPs) using for the first time an alkaline protease (ALPs) derived from Phalaris minor seed extract. A series of physicochemical techniques were used to inquire the formation, size, shape and crystalline nature of ALPs-AuNPs. The nanoparticles' ability to degrade methylene blue (MB) through photocatalysis under visible light irradiation was assessed. The findings demonstrated that ALPs-AuNPs exhibited remarkable efficacy by destroying 100 % of MB within a mere 30-minute irradiation period. In addition, the ALPs-AuNPs demonstrated remarkable effectiveness in inhibiting the growth of gram-positive (S. aureus) and gram-negative (E. coli) bacteria. The inhibition zones examined against the two bacterial strains were 23(±0.3) mm and 19(±0.4); 13(±0.3) mm and 11(±0.5) mm under light and dark conditions respectively. The ALPs-AuNPs exhibited significant antioxidant activity by effectively scavenging 88 % of stable and 2,2-diphenyl-1-picrylhydrazyl (DPPH) radicals. As a result, the findings demonstrated that the environmentally friendly ALPs-AuNPs showed a strong potential for MB degradation and bacterial pathogen treatment.
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http://dx.doi.org/10.1016/j.ijbiomac.2024.131067 | DOI Listing |
Int J Biol Macromol
January 2025
Nitte (Deemed to be University), Nitte University Centre for Science Education and Research, Department of Bio & Nano Technology, Paneer Campus, Deralakatte, Mangaluru 575018, Karnataka, India. Electronic address:
Bacteriophages, the most abundant biological agents targeting bacteria, offer a promising alternative to antibiotics for combating multi-drug resistant pathogens like Acinetobacter baumannii. However, the rapid development of bacteriophage resistance poses a significant challenge. This study highlights the contribution of outer membrane proteins (OMPs) in the emergence of bacteriophage resistance in A.
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January 2025
Department of Molecular Biology and Genetics, Faculty of Science, Ataturk University, 25240, Erzurum, Turkey. Electronic address:
Recycling of protein-rich environmental wastes and obtaining more valuable products from these recycled products is a topic of interest for researchers. This study aims to produce, purify, and characterize the physicochemical and structural properties of the protease enzyme produced from Brevibacillus agri SAR25 using salmon fish waste as substrate and also to evaluate the effect of protease on the chicken feather, enzyme-ligand interactions, and active site surface area. The production of protease was optimum on 50 g/L fish waste, pH 8, 40 °C, 96 h, and 150 rpm.
View Article and Find Full Text PDFArch Dermatol Res
January 2025
Department of Biotechnology, Institute of Graduate Studies and Research, Alexandria University, Alexandria, 21526, Egypt.
J Fungi (Basel)
December 2024
College of Food Sciences and Technology, Shanghai Ocean University, Shanghai 201306, China.
is a tasty and low-calorie mushroom containing abundant high-quality protein. This study aims to improve the digestibility of protein (PEP) and hence to facilitate its development as a healthy alternative protein. The extracted PEP was pretreated with 1000-5000 U of papain, neutral protease and alkaline protease.
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November 2024
Guangxi Key Laboratory of Beibu Gulf Marine Biodiversity Conservation, Beibu Gulf University, Qinzhou 535011, China.
Crustins are a family of antimicrobial peptides (AMPs) that play a pivotal role in the innate immune system of crustaceans. The discovery of novel AMPs from natural sources is crucial for expanding our current database of these peptides. Here, we identified and characterized a novel member of the crustin family, named Crus-SWD1, derived from .
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