作者: Eduardo Barzana , Marcus Karel , Alexander M. Klibanov
关键词: Enzyme assay 、 Substrate (chemistry) 、 Inorganic chemistry 、 Acetaldehyde 、 Ethanol 、 Catalysis 、 Aqueous solution 、 Alcohol oxidase 、 Water activity 、 Stereochemistry 、 Chemistry
摘要: The enzymatic conversion of gaseous substrates represents a novel concept in bioprocessing. A critical parameter such systems is the water activity, Aw present article reports effect on catalytic performance alcohol oxidase acting ethanol vapors. Enzyme activity gas-phase reaction increases several orders magnitude, whereas thermostability decreases drastically when increased from 0.11 to 0.97. enzyme active even at hydration levels below monolayer coverage. Enhanced lower hydrations results an increase optimum temperature catalyzed by oxidase. apparent activation energy as increases, approaching value obtained for aqueous solution. formation pread-sorbed phase surface support not prerequisite reaction, suggesting that occurs direct interaction substrate with enzyme. follows Michaelis–Menten kinetics, Km almost 100 times than Based vapor–liquid equilibrium data and observed values, it postulated during establishes vapor similar between gas phase.