Purification and biochemical characterization of a nattokinase by conversion of shrimp shell with Bacillus subtilis TKU007

San Lang Wang, Ying Ying Wu, Tzu Wen Liang

研究成果: Article同行評審

66 引文 斯高帕斯(Scopus)

摘要

BSN1, a nattokinase, was purified from the culture supernatant of Bacillus subtilis TKU007 with shrimp shell wastes as the sole carbon/nitrogen source. The BSN1 was purified to homogeneity by three-step procedure with a 515-fold increase in specific activity and 12% recovery. The molecular masses of BSN1 determined by SDS-PAGE and gel filtrations were approximately 30. kDa and 28. kDa, respectively. The results of peptide mass mapping showed that four tryptic peptides of BSN1 were identical to the nattokinase from B. subtilis (GenBank accession number gi14422313) with 37% sequence coverage. The N-terminal amino acid sequence of the first 12 amino acids of BSN1 was AQSVPYGISQIK. The optimum pH, optimum temperature, pH stability, and thermal stability of BSN1 were 8, 40°C, pH 4-11, and less than 50°C, respectively. BSN1 was inhibited completely by PMSF, indicating that the BSN1 was a serine protease. Using this method, B. subtilis TKU007 produces a nattokinase/fibrinolytic enzyme and this enzyme may be considered as a new source for thrombolytic agents.

原文English
頁(從 - 到)196-202
頁數7
期刊New Biotechnology
28
發行號2
DOIs
出版狀態Published - 2011 2月 28

All Science Journal Classification (ASJC) codes

  • 生物技術
  • 生物工程
  • 分子生物學

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