L-Glutathione Reduced was first discovered in yeast by French scientist Rey-Pailhade in 1888 and was named "philothion". Then Hopkins discovered in 1921 that it was self-oxidizing and contained glutamic acid and cysteine, and changed its name to"L-Glutathione Reduced". With the development of crystal formation technology, L-Glutathione Reduced was determined to be a tripeptide composed of glutamic acid, cysteineand glycine in 1929. It was originally discovered in a variety of biological tissues. Solvent extraction can be used to obtain L-Glutathione Reduced from animal and plant tissues. However, due to the limitation of raw materials and low intracellular concentration, L-Glutathione Reduced is expensive, which hinders its practical application. In 1935, Harington et al. synthesized L-Glutathione Reduced by chemical methods, and then optimized chemical synthesis methods realized the commercialization of L-Glutathione Reduced, but the chemically synthesized products are a mixture of optical isomers, and only the L configuration has physiological activity The introduction and removal of sulfhydryl protecting agents on cysteineresidues are key steps in chemical synthesis. The biosynthesis of L-Glutathione Reduced is based on the incubation reaction of isotope-labeled glutamic acid and glycine with isolated liver tissue, and it is determined that it is synthesized by a two-step enzymatic catalytic reaction, and Meister clarified that L-Glutathione Reduced is composed of two ATPs. Relying on the pathway of GSH I and GSH II catalyzed synthesis, finally realized the production of L-Glutathione Reduced by enzymatic method or fermentation method. Among them, Japanese scientists have conducted a lot of research on the production of L-Glutathione Reduced by enzyme method and fermentation method, and in the early 1980s, the commercial production of L-Glutathione Reduced by yeast fermentation method was carried out.