枯草芽孢杆菌 YJ1 来源纳豆激酶的生物特性。

Bioproperties of potent nattokinase from Bacillus subtilis YJ1.

机构信息

Department of Sea Food Science, National Kaohsiung Marine University, Nan-Tzu, Kaohsiung, Taiwan.

出版信息

J Agric Food Chem. 2010 May 12;58(9):5737-42. doi: 10.1021/jf100290h.

PMID:20334345

Abstract

Fibrinolytic enzyme activity was observed during cultivation of Bacillus subtilis YJ1 in a medium containing 1% skim milk, 1% rice husk, 0.5% NaCl, and 0.25% glucose. It was purified to electrophoretical homogeneity after CM-sepharose FF chromatography. The specific activity and yield were 1791.9 FU/mg and 9.5%, respectively. This purified fibrinolytic enzyme had M of 27.5 kDa, optimal temperature and pH at 50 degrees C and 8.5, respectively. It was stable at pH 6.0-10.0 and 10-40 degrees C and inhibited by Fe(3+), Hg(2+), Cu(2+), Zn(2+), and PMSF. Compared the N terminal of amino acids and full DNA sequence with those in NCBI, it was considered to be a nattokinase.

摘要

在含有 1%脱脂乳、1%稻壳、0.5%NaCl 和 0.25%葡萄糖的培养基中培养枯草芽孢杆菌 YJ1 时，观察到纤维蛋白溶酶活性。该酶经 CM-琼脂糖 FF 层析纯化至电泳均一性。比活和得率分别为 1791.9 FU/mg 和 9.5%。该纯化的纤维蛋白溶酶的 M r 为 27.5 kDa，最适温度和 pH 值分别为 50°C 和 8.5。它在 pH 值 6.0-10.0 和 10-40°C 之间稳定，并被 Fe(3+)、Hg(2+)、Cu(2+)、Zn(2+) 和 PMSF 抑制。与 NCBI 中的 N 末端氨基酸和全长 DNA 序列相比，它被认为是纳豆激酶。