Continuous hydrolysis of 4-cyanopyridine by nitrilases from Fusarium solani O1 and Aspergillus niger K10
Applied Microbiology and Biotechnology, ISSN: 0175-7598, Vol: 85, Issue: 2, Page: 277-284
2009
- 41Citations
- 43Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations41
- Citation Indexes41
- 41
- CrossRef34
- Captures43
- Readers43
- 43
Article Description
The operational stabilities of nitrilases from Aspergillus niger K10 and Fusarium solani O1 were examined with 4-cyanopyridine as the substrate in continuous-stirred membrane reactors (CSMRs). The former enzyme was fairly stable at 30 °C with a deactivation constant (k ) and enzyme half-life of 0.014 h and 50 h, respectively, but the latter exhibited an even higher stability characterized by k ∈= ∈0.008 h and half-life of 87 h at 40 °C. Another advantage of this enzyme was its high chemoselectivity, i.e., selective transformation of nitriles into carboxylic acids, while the amide formed a high ratio of A. niger K10 nitrilase product. High conversion rates (>90%) were maintained for about 52 h using the nitrilase from F. solani O1 immobilized in cross-linked enzyme aggregates (CLEAs). The purity of isonicotinic acid was increased from 98% to >99.9% by using two CSMRs connected in series, the first one containing the F. solani O1 nitrilase and the second the amidase from Rhodococcus erythropolis A4 (both enzymes as CLEAs), the amidase hydrolyzing the by-product isonicotinamide. © 2009 Springer-Verlag.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=71349084019&origin=inward; http://dx.doi.org/10.1007/s00253-009-2073-x; http://www.ncbi.nlm.nih.gov/pubmed/19554325; http://link.springer.com/10.1007/s00253-009-2073-x; http://www.springerlink.com/index/10.1007/s00253-009-2073-x; http://www.springerlink.com/index/pdf/10.1007/s00253-009-2073-x; https://dx.doi.org/10.1007/s00253-009-2073-x; https://link.springer.com/article/10.1007/s00253-009-2073-x
Springer Science and Business Media LLC
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