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

두유응고효소 I 및 II에 의한 11S 단백질(Glycinin)의 가수분해 패턴

Hydrolytic patterns of 11S globulin (glycinin), storage protein of soybean, by soymilk-clotting enzymes Iand IIfrom 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 Iand II(0.025 units at 35$^{\circ}C$) on the acidic subunit. In electrophoresis, acidic subunit (A$_3$, 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.

박테리아 Bacillus sp. K-295G-7이 생산하는 두유응고효소 I 및 II에 의한 11S globulin (glycinin)의 가수분해 패턴을 조사하였다. 효소 I 과 II에 의한 acidic subunit의 응고시간은 약 4-5 분이었다. 전기 영동의 결과, acidic subunit (A$_3$, M.W=45,000)는 효소반응 2분 이내에 완전히 가수분해되어 분자량 16,000, 20,000의 새로운 band를 형성하였다. 한편 효소 II의 작용으로 약 30,000의 분자량을 가진 분해산물을 생성하였고 효소 I 과 II의 basic subunit 에 대한 가수분해 패턴은 유사하였다.