Characterization and kinetics of lipase inhibitory activity of streptomyces tendae

Abstract

The Streptomyces tendae was grown in the submerged cultures and the lipase inhibitory activity was assyed by using porcine pancreatic lipase. The inhibitory activity was extracted with ethyl acetate and purified by using HPLC. The inhibitory activity was characterized by UV-Vis spectrophotometry and LC-MS and its kinetic studies were done with Lineweaver-Burk plots. Lipase inhibitory activity was identified in the submerged cultures of S. tendae and its productivity was higher on the 7^th day of fermentation. This inhibitory activity was eluted into the diethyl ether fraction while purifying on silica gel chromatogram and purified compound showed a single peak on HPLC. The compound showed the λ_max of 254 nm, IC₅₀ of 147.58 μg/ml and mass of 254 amu. Mass suggested it as a small molecule. Kinetic studies suggested that this molecule inhibits the porcine pancreatic lipase in a competitive manner.