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Identification of Novel Bacillus subtilis IDCC 9204 Producing a High-Level Fibrinolytic Enzyme and Properties of NK-IL9204

机译:新型枯草芽孢杆菌IDCC 9204产生高水平的纤溶酶的鉴定及NK-IL9204的特性

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摘要

A Bacillus sp. that produces fibrinolytic enzyme was isolated from Cheonggukjang, a traditional Korean soybean-fermented food. According to 16S rRNA gene base sequencing, the bacillus was identified as a variety of Bacillus subtilis, and named Bacillus subtilis IDCC 9204. Fibrinolytic enzyme NK-IL9204 was stable up to 60°C and within pH range of 5-10. Purified NK-IL9204 was detected through fibrin zymography. The molecular weight and isoelectric point of the enzyme were estimated to be 27.7 kDa and6.7 by SDS-PAGE and 2D electrophoresis, respectively. Its amino acid sequence was similar to that of nattokinase (identities 99.5%) and different from that of nattokinase BPN (identities 86.4%). The plasma fibrinolytic activity of NK-IL9204 was measuredby euglobulin clot lysis times (ECLT). The NK-IL9204 was orally administered to SD rats for 3 weeks (1,000 FU/rat/day). The ECLT was significantly shortened by supplementation of NK-IL9204.
机译:芽孢杆菌从韩国传统大豆发酵食品清谷酱中分离出产生纤溶酶的酶。根据16S rRNA基因碱基测序,该杆菌被鉴定为多种枯草芽孢杆菌,并命名为枯草芽孢杆菌IDCC9204。纤溶酶NK-IL9204在高达60°C的温度和5-10的pH范围内均稳定。通过纤维蛋白酶谱法检测纯化的NK-IL9204。通过SDS-PAGE和2D电泳估计该酶的分子量和等电点分别为27.7 kDa和6.7。其氨基酸序列与纳豆激酶相似(同一性为99.5%),与纳豆激酶BPN相似(同一性为86.4%)。通过球蛋白凝块溶解时间(ECLT)测量NK-IL9204的血浆纤维蛋白溶解活性。将NK-IL9204口服给予SD大鼠3周(1,000 FU /大鼠/天)。补充NK-IL9204可大大缩短ECLT。

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