Quantitative spectrophotometric assay for staphylococcal lipase

Article Abstract:

Quantitative assays for lipase activity are generally complicated procedures requiring the use of specialized instruments. A simple, less expensive procedure for the quantitative determination of lipase activity in culture supernatants of Staphylococcus aureus was developed. The procedure exploits the ability of lipase to induce clearing of tributyrin emulsions. Tributyrin clearance is measured in plate assays by spectorphotometric analysis. Tests showed that the procedure is sensitive to 1.0 micrograms of lipase per milliliter, and under the prescribed conditions, is specific for lipase detection.

Methods, Analysis, Usage, Staphylococcus aureus, Tributyltin, Lipase, Spectrophotometry, Tributylin

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Purification and partial characterization of a novel antibacterial agent (Bac1829) produced by Staphylococcus aureus KSI1829

Article Abstract:

Staphylococcus aureus KSI1829 produces an antibacterial agent, Bac1829, that is a bacteriocin-like heat stable substance showing activity against different genera of microorganisms. The digestive action of proteases kills this peptide. The stability of Bac1829 is similar to that of other gram-positive bacteriocins. Bac1829 is hydrophobic due to the presence of a large number of hydrophobic amino acids. Purified Bac1829 destroys exponentially growing Corynebacterium renale by a bactericidal mode of action.

Antibacterial agents, Staphylococcus

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Purification and characterization of staphylococcin BacR1, a broad-spectrum bacteriocin

Article Abstract:

The broad-spectrum bacteriocin, staphylococcin BacR1 is purified and characterized by molecular weight determination, amino acid composition and mode of action. This bacteriocin appears to interact with a specific cellular receptor. Staphylococcin BacR1 was found to be bactericidal against many microorganisms. The therapeutic implications of its bactericidal activity are elucidated.

Health aspects, Bacterial proteins, Pharmaceutical microbiology

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