Serratiopeptidase derived from S. marcescens SP6 underwent a four-step purification process, resulting in a 15.91-fold increase in purity, and exhibited resistance to degradation by trypsin and serum, suggesting its possible use as an adjunct therapeutic agent alongside conventional antimicrobials to combat biofilm-associated infections.
The widespread prevalence of methicillin-resistant Staphylococcus aureus (MRSA) in community and healthcare settings has driven the urgent search for novel antibacterial agents. Mangrove sediments are an underexplored source of antimicrobial-producing bacteria. This study characterized an antimicrobial fraction and the...
These findings provide an efficient purification protocol for pediocin PA-1 and comprehensively characterize its stability and antimicrobial kinetics, supporting its potential as a natural food preservative.
Jian-Min Song, Xiao-Jing Ma, Juan Bai et al.· Preparative Biochemistry & B...· 0 citations
Keratinases are specialized proteases capable of degrading recalcitrant keratin and have attracted considerable interest for environmentally sustainable bioprocessing. In this study, a keratinase gene from Bacillus tequilensis strain YIV, isolated from tannery waste in Kasur, Pakistan, was cloned, expressed, and charac...
Noor e Hira, I. Haq, M. Aftab· International Journal of Bio...· 0 citations
In vitro findings indicate potential applicability of SO7 α-amylase in high-temperature and alkaline bioprocesses; however, solvent tolerance was assessed only under the tested short-term conditions, and performance under real industrial process conditions remains to be validated.
Sultan Sevinc, Sumeyye Akbulut, Esra Aygun et al.· 3 Biotech· 0 citations
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