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Beta-lactamases are enzymes produced by pathogenic microorganisms which exhibit resistance to beta-lactam group of antibiotics and are of considerable clinical importance. In our study, we examined the pathogenic organisms for the secretion of beta-lactamase using the antibiotic ampicillin. The extracted beta-lactamase from the isolates was characterized biochemically for enzyme activity and to initiate their inhibition activities.  The protein extracts separated from the potential actinomycetes species were analyzed by targeting against the beta lactamase enzyme activity. The beta-lactamase enzymes from bacterial isolates were purified from the cell free culture extract and activity was estimated spectrophotometrically.    The actinomycetes isolated from the soil source were tested for their efficiency to inhibit the beta-lactamase enzyme activity. The protein fractions were extracted by salt precipitation using ammonium sulfate and further salt removal by dialysis technique. The assays for enzyme inhibition were performed by plate well diffusion along with absorbance readings of the enzyme and substrate using spectrophotometer. The beta-lactamase enzyme activity of  Proteus  sp. had shown highest enzymatic activity followed by  Staphylococcus aureus  and  Pseudomonas  sp .  The protein extracts of four actinomycetes isolates that showed beta-lactamase inhibition were identified belonging to the genus  Streptomyces  based on their colony morphology, microscopic observation, and biochemical tests. The beta-lactamase inhibition activities were analyzed to combat antibiotitc resistances exerted by the pathogenic bacteria in infections.   

Protein extracts from <em>streptomyces</em> sps. inhibits beta-lactamases secreted by pathogenic bacteria