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

Paper ID Volume ID Publish Year Pages File Format Full-Text
33456 44979 2011 7 PDF Available
Title
Purification and biochemical characterization of a nattokinase by conversion of shrimp shell with Bacillus subtilis TKU007
Abstract

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.

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Purification and biochemical characterization of a nattokinase by conversion of shrimp shell with Bacillus subtilis TKU007
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Publisher
Database: Elsevier - ScienceDirect
Journal: New Biotechnology - Volume 28, Issue 2, 28 February 2011, Pages 196–202
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
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