title: Partial purification and characterization of lipase from Geobacillus stearothermophilus AH22.
abstract: The lipase was partially purified by ion exchange chromatography and gel filtration column chromatography, and was characterized from Geobacillus stearothermophilus AH22 strain. The lipase was purified 18.3-folds with 19.7% recovery. The lipase activity was determined by using p-nitrophenyl esters (C2-C12) as substrates. The Km values of the enzyme for these substrates were found as 0.16, 0.02, 0.19 and 0.55 mM, respectively, while Vmax values were 0.52, 1.03, 0.72 and 0.15 U mg(-1). The enzyme showed maximum activity at 50 °C and between pH 8.0 and 9.0. The enzyme was found to be quite stable at pH range of 4.0-10.0, and thermal stability between 50 and 60 °C. It was found that the best inhibitory effect of the enzyme activity was of Hg(2+). The inhibitory effect as orlistat, catechin, propyl paraben, p-coumaric acid, 3,4-dihydroxy hydro-cinnamic acid was examined. These results suggest that G. stearothermophilus AH22 lipase presents very suitable properties for industrial applications.
authors: a Department of Chemistry, Faculty of Arts and Sciences , Recep Tayyip Erdoğan University , Rize , Turkey and.
authors: Arife Pınar
authors: AP
authors: Ekinci
authors: a Department of Chemistry, Faculty of Arts and Sciences , Recep Tayyip Erdoğan University , Rize , Turkey and.
authors: Barbaros
authors: B
authors: Dinçer
authors: a Department of Chemistry, Faculty of Arts and Sciences , Recep Tayyip Erdoğan University , Rize , Turkey and.
authors: Nimet
authors: N
authors: Baltaş
authors: b Department of Molecular Biology and Genetic, Faculty of Science , Atatürk University , Erzurum , Turkey.
authors: Ahmet
authors: A
authors: Adıgüzel
mesh_terms: D001426:Bacterial Proteins / Q000302:isolation & purification / Q000378:metabolism; D002392:Catechin / Q000494:pharmacology; D003373:Coumaric Acids; D004591:Electrophoresis, Polyacrylamide Gel; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004795:Enzyme Stability; D001411:Geobacillus stearothermophilus / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007783:Lactones / Q000494:pharmacology; D008049:Lipase / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism*; D008670:Metals / Q000737:chemistry / Q000494:pharmacology; D000077403:Orlistat; D010226:Parabens / Q000494:pharmacology; D011422:Propionates / Q000494:pharmacology; D013501:Surface-Active Agents / Q000737:chemistry; D013696:Temperature
chemical_list: D001426:Bacterial Proteins; D003373:Coumaric Acids; D004791:Enzyme Inhibitors; D007783:Lactones; D008670:Metals; D010226:Parabens; D011422:Propionates; D013501:Surface-Active Agents; D002392:Catechin; D000077403:Orlistat; D008049:Lipase; C495469:p-coumaric acid; C006068:propylparaben
keywords: Characterization; Geobacillus stearothermophilus AH22; lipase; partial purification