ArticleJournal of industrial microbiology & biotechnology2010
Preparation of carboxylated magnetic particles for the efficient immobilization of C-terminally lysine-tagged Bacillus stearothermophilus aminopeptidase II.
Article in Journal of industrial microbiology & biotechnology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- MHJ_0461 is a multifunctional leucine aminopeptidase on the surface of Mycoplasma hyopneumoniae.Open biology · 2015Article
- Surface-functionalized hyperbranched poly(amido acid) magnetic nanocarriers for covalent immobilization of a bacterial γ-glutamyltranspeptidase.Molecules (Basel, Switzerland) · 2014Article
- Covalent Immobilization of Bacillus licheniformis γ-Glutamyl Transpeptidase on Aldehyde-Functionalized Magnetic Nanoparticles.International journal of molecular sciences · 2013Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
This article reports the synthesis and use of surface-modified iron oxide particles for the simultaneous purification and immobilization of Bacillus stearothermophilus aminopeptidase II (BsAPII) tagged C-terminally with either tri- or nona-lysines (BsAPII-Lys(3/9)). The carboxylated magnetic particles were prepared by the simple co-precipitation of Fe(3+)/Fe(2+) in aqueous medium and then subsequently modified with adipic acid. Transmission electron microscopy (TEM) micrographs showed that the carboxylated magnetic particles remained discrete and had no significant change in size after binding BsAPIIs. Wild-type enzyme and BsAPII-Lys(3) could be purified to near homogeneity by the carboxylated magnetic particles, but it was not easy to elute the adsorbed BsAPII-Lys(9) from the matrix. Free BsAPII, BsAPII-Lys(3), and BsAPII-Lys(9) were active in the temperature range 50-70 degrees C and all had an optimum of 50 degrees C, whereas the optimum temperature and thermal stability of BsAPII-Lys(3) and BsAPII-Lys(9) were improved as a result of immobilization. The immobilized BsAPII-Lys(9) could be recycled ten times without a significant loss of the enzyme activity and had a better stability during storage than BsAPII. Owing to its high efficiency and cost-effectiveness, this magnetic adsorbent may be used as a novel purification-immobilization system for the positively charged enzymes.
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20373125What OpenQuestion holds
Registered trials
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