Purification, immobilization, and characterization of nattokinase on PHB nanoparticles
In this study, nattokinase was purified from Bacillus subtilis using ion exchange chromatography and immobilized upon polyhydroxybutyrate (PHB) nanoparticles. A novel strain isolated from industrial dairy waste was found to synthesize polyhydroxyalkanoates (PHA) and the strain was identified as Brev...
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Veröffentlicht in: | Bioresource technology 2009-12, Vol.100 (24), p.6644-6646 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | In this study, nattokinase was purified from
Bacillus
subtilis using ion exchange chromatography and immobilized upon polyhydroxybutyrate (PHB) nanoparticles. A novel strain isolated from industrial dairy waste was found to synthesize polyhydroxyalkanoates (PHA) and the strain was identified as
Brevibacterium
casei SRKP2. PHA granules were extracted from 48
h culture and the FT-IR analysis characterized them as PHB, a natural biopolymer from
B.
casei. Nanoprecipitation by solvent displacement technique was used to synthesize PHB nanoparticles. PHB nanoparticles were characterized using transmission electron microscopy and particle size ranged from 100–125
nm. Immobilization of nattokinase upon PHB nanoparticles resulted in a 20% increase in the enzyme activity. Immobilization also contributed to the enhanced stability of the enzyme. Moreover, the activity was completely retained on storage at 4
°C for 25
days. The method has proven to be highly simple and can be implemented to other enzymes also. |
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ISSN: | 0960-8524 1873-2976 |
DOI: | 10.1016/j.biortech.2009.06.057 |