Hydrolytic Patterns of 11S Globulin(Glycinin) by Soymilk - Clotting Enzymes Ⅰ and Ⅱ

국문 초록 (Abstract)

박테리아 Bacillus sp. K-295G-7이 생산하는 두유응고효소 Ⅰ 및 Ⅱ에 의한 11S globulin(glycinin)의 가수분해 패턴을 조사하였다. 효소 Ⅰ과 Ⅱ에 의한 acidic subunit의 응고시간은 약 4~5 분 이었다. 전기영동의 결과, acidic subunit(A₃, MW=45,000)는 효소반응 2분 이내에 완전히 가수분해 되어 분자량 16,000, 20,000의 새로운 band를 형성하였다. 한편 효소 Ⅱ의 작용으로 약 30,000의 분자량을 가진 분해산물을 생성하였고, 효소 Ⅰ과 Ⅱ의 basic subunit에 대한 가수분해 패턴은 유사하였다.

다국어 초록 (Multilingual Abstract)

Hydrolytic patterns of 11S globulin(glycinin), storage protein of soybean, by soymilk-clotting enzymes Ⅰ and Ⅱ from Bacillus sp. K-295G-7, which was the first soymilk-clotting enzyme to be found in a bacteria, was investigated. The clotting time of about 4~5 min is revealed by the Enzymes Ⅰ and Ⅱ(0.025 units at 35℃) on the acidic subunit. In electrophoresis, acidic subunit(A₃, M.W. 45,000) disappeared almost completely within 2 min and new products corresponding to the molecular weight of 16,000 and 20,000 were formed by the action of Enzymes Ⅰ and Ⅱ. Furthermore, Enzyme Ⅱ produced a degradation compound having a molecular weight of about 30,000. In contrast, the hydrolytic patterns of basic subunit (M.W. 20,000) by Enzymes Ⅰ and Ⅱ were similar, but Enzyme Ⅱ produced low molecular weight products slower than that of Enzyme Ⅰ.

목차 (Table of Contents)

• Abstract
  
• INTRODUCTION
  
• MATERIALS AND METHODS
  
• RESULTS AND DISCUSSION
  
• REFERENCES
  
• 요약