Nitrile hydratase of Rhodococcus erythropolis: characterization of the enzyme and the use of whole cells for biotransformation of nitriles

Content Provider	Semantic Scholar
Author	Kamble, Ashwini L. Banoth, Linga Meena, Vachan Singh Singh, Amit Chisti, Yusuf Banerjee, Uttam Chand
Copyright Year	2012
Abstract	The intracellular cobalt-type nitrile hydratase was purified from the bacterium Rhodococcuserythropolis. The pure enzyme consisted of two subunits of 29 and 30 kDa. The molecular weight of the native enzyme was estimated to be 65 kDa. At 25 °C the enzyme had a half-life of 25 h. The Michaelis–Menten constants Km and vmax for the enzyme were 0.624 mM and 5.12 μmol/min/mg, respectively, using 3-cyanopyridine as the substrate. The enzyme-containing freely-suspended bacterial cells and the cells immobilized within alginate beads were evaluated for converting the various nitriles to amides. In a packed bed reactor, alginate beads (2 % alginate; 3 mm bead diameter) containing 200 mg/mL of cells, achieved a conversion of >90 % for benzonitrile and 4-cyanopyridine in 38 h (25 °C, pH 7.0) at a feed substrate concentration of 100 mM. The beads could be reused for up to six reaction cycles.
Starting Page	319
Ending Page	330
Page Count	12
File Format	PDF HTM / HTML
DOI	10.1007/s13205-012-0104-2
PubMed reference number	28324592
Journal	Medline
Volume Number	3
Alternate Webpage(s)	http://ftp.ncbi.nlm.nih.gov/pub/pmc/87/90/13205_2012_Article_104.PMC3723861.pdf
Alternate Webpage(s)	https://rd.springer.com/content/pdf/10.1007%2Fs13205-012-0104-2.pdf
Alternate Webpage(s)	https://doi.org/10.1007/s13205-012-0104-2
Journal	3 Biotech
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article