{'fraction_non_alphanumeric': 0.03733121525019857, 'fraction_numerical': 0.017474185861795076, 'mean_word_length': 4.701357466063349, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Study on the Activity of Lipase Catalyzing Hydrolytic Reaction of Glycerol α-Monostearate in a Water-in-Oil Microemulsion

The lipase-catalyzed hydrolytic reaction of glycerol α-monostearate as substrate in a water-in-oil (W/O) microemulsion was first studied. Results indicated that, for a W/O microemulsion composed of n-heptane, water and sodium bis (2-ethylhexyl) sulfosuccinate (AOT), the pH value and the ionic strength of the phosphate buffer, the ω 0 value and the AOT concentration had an effect on the activity of lipase. The optimum values of these parameters were as follows: 1) the pH value was 7.17 with the concentration of the phosphate buffer being 0.067 mol/L; 2) the ω 0 value was 8;and 3) the concentration of AOT was 0.10 mol/L. Kinetic studies showed that the reaction mechanism in the microemulsion was the same as that in water. At a constant concentration of lipase, the relationship between the reaction rate and the concentration of the substrate could be expressed as Michaelis-Menten equation. The maximum rate and the Michaelis constant were about 156u (expressed as the activity of lipase) and 5.6 mmol/L, respectively. At a constant concentration of substrate, the rate was directly proportional to the concentration of lipase.