Abstract: A method for improving uniformity of an electromagnetic field inside a static microwave resonant cavity is provided. The overlap between a nodal point in one mode and an antinodal point in another node inside a microwave resonant cavity is realized by using two different types of anisotropic media, thereby improving distribution uniformity of an electromagnetic field inside a static resonant cavity. The method can reduce the complexity of cavity mechanisms of a microwave oven having a turntable and a flat panel microwave having an electromagnetic stirrer and improve static microwave treatment uniformity, thereby promoting the application of high-temperature and high-power microwave treatment in the fields such as microwave sintering, microwave smelting, and microwave chemical industry.

Abstract: A method for improving uniformity of an electromagnetic field inside a static microwave resonant cavity is provided. The overlap between a nodal point in one mode and an antinodal point in another node inside a microwave resonant cavity is realized by using two different types of anisotropic media, thereby improving distribution uniformity of an electromagnetic field inside a static resonant cavity. The method can reduce the complexity of cavity mechanisms of a microwave oven having a turntable and a flat panel microwave having an electromagnetic stirrer and improve static microwave treatment uniformity, thereby promoting the application of high-temperature and high-power microwave treatment in the fields such as microwave sintering, microwave smelting, and microwave chemical industry.

Abstract: A selenium-chelating pea oligopeptide, a preparation method thereof and use thereof. After the selenium-chelating pea oligopeptide is subjected to digestion treatment in at least one of following three ways, a change rate of selenium content not more than 3% with respect to the selenium content before the digestion treatment: hydrolyzing for 4 hours by a pepsin at a pH value of 2 and a temperature of 37° C.; hydrolyzing for 6 hours by a trypsin at a pH value of 7.5 and a temperature of 37° C.; maintaining the temperature constant at 37° C., firstly hydrolyzing for 4 hours by the pepsin at a pH value of 2, and then continuing to hydrolyze for 6 hours by a trypsin at a pH value of 6.8. The preparation method thereof includes mixing and reacting an aqueous solution of pea oligopeptide and sodium selenite, and then being subjected to alcohol precipitation and drying.