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고농도 혈전용해효소를 생산하는 신규 Bacillus subtilis IDCC 9204의 분리 및 NK-IL9204의 효소학적 특성
이승훈(Seung-Hun Lee),안광민(Gwangmin An),김희항(Heu-Hang Kim),강재훈(Jae-Hoon Kang),강대중(Dae-Jung Kang) 한국식품과학회 2012 한국식품과학회지 Vol.44 No.5
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 60oC 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 and 6.7 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 measured by euglobulin clot lysis times (ECLT). The NKIL9204 was orally administered to SD rats for 3 weeks (1,000 FU/rat/day). The ECLT was significantly shortened by supplementation of NK-IL9204.