Soybeans are a traditional food in eastern Asia, particularly in Japan and China. They were eaten in 100 BC in China. The beans can be processed into Tofu, soy milk, fermented seasonings, soy sauce or Miso paste, and Natto and green beans. Soybeans have rich nutrition, protein lipid, and other functional substances such as isoflavones. However, soybeans are difficult to process for use as food because of tissue and cell wall hardness. Therefore, soybeans are conducted to do some treatments, e.g., boiling, steaming, roasting, crushing/grinding, and some enzyme treating, to eat soy protein easily. Soy storage proteins mainly comprise two proteins as 7S globulin composed with β-conglycinin and 11S globulin containing glycinin composed of 5 subunits. β-Conglycinin, included in 7S globulin, is composed of three subunits. To modify the physical properties of soy protein, a new type of enzyme for curdling soybean milk enzyme was purified as an extract from yeast. Yeast producing curdling soybean milk enzyme, the SCY003 strain, was isolated from 1345 yeast strains. According to the morphology, physiology, and molecular and characteristics, SCY003 was identified as Saccharomyces bayanus. The soy milk curdling enzyme having proteolytic activity was approximately 45 kDa and monomer protein. The optimum pH for the protease activity was pH 7.5; the optimum temperature was 50°C. The enzyme cleaved the β-conglycinin as α-, α′-, and part of glycinin as A 3 A 4 , A 1b , and A 2 in soy protein by endoproteolysis. Soybean protein became loosely curdled with the addition of other proteases from microorganisms or plants. Soybean milk curdled after cleaving endoproteolysis enzyme in SCY003 strain.