Biotransformation of nitriles using the solvent-tolerant nitrile hydratase from Rhodopseudomonas palustris CGA009

Black, Gary W.; Gregson, Thomas J.; McPake, Christopher B.; Perry, Justin J.; Zhang, Meng

doi:10.1016/j.tetlet.2009.12.094

Cited by 19 publications

(17 citation statements)

References 8 publications

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“…mediately in the vicinity of the nitrile to affect the capacity of NHase to hydrolyse these small aromatic substrates. This finding is suppor eric hindrance caused problems with conversion of 2,6-disubstituted benzonitriles for a purified NHase from a strain of Rhodopseudom 2,6-difluorobenzonitrile was readily converted, while replacement of the F atoms with the larger chlorine atoms in 2,6-dichloroben lobenil) reduced conversion to a negligible level [32]. This clearly points to steric hindrance rather than electronic effects being respo ctivity of the two substrates.…”

Section: Resultsmentioning

confidence: 89%

Substrate Profiling of the Cobalt Nitrile Hydratase from Rhodococcus rhodochrous ATCC BAA 870

et al. 2020

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The aromatic substrate profile of the cobalt nitrile hydratase from Rhodococcus rhodochrous ATCC BAA 870 was evaluated against a wide range of nitrile containing compounds (>60). To determine the substrate limits of this enzyme, compounds ranging in size from small (90 Da) to large (325 Da) were evaluated. Larger compounds included those with a bi-aryl axis, prepared by the Suzuki coupling reaction, Morita–Baylis–Hillman adducts, heteroatom-linked diarylpyridines prepared by Buchwald–Hartwig cross-coupling reactions and imidazo[1,2-a]pyridines prepared by the Groebke–Blackburn–Bienaymé multicomponent reaction. The enzyme active site was moderately accommodating, accepting almost all of the small aromatic nitriles, the diarylpyridines and most of the bi-aryl compounds and Morita–Baylis–Hillman products but not the Groebke–Blackburn–Bienaymé products. Nitrile conversion was influenced by steric hindrance around the cyano group, the presence of electron donating groups (e.g., methoxy) on the aromatic ring, and the overall size of the compound.

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Section: Resultsmentioning

confidence: 89%

Substrate Profiling of the Cobalt Nitrile Hydratase from Rhodococcus rhodochrous ATCC BAA 870

et al. 2020

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“…Aqueous media can limit the use of nitrile hydrolysing enzymes in the hydration of inherently hydrophobic nitriles, though added quantities of organic solvents can be used to aid substrate availability to the enzyme in some cases . Several solvent based approaches have been reported in the literature including monophasic systems with solvents such as DMSO and biphasic systems such as toluene/H 2 O and hexane/H 2 O and some systems can operate in both buffer‐organic solvent monophasic or biphasic mixtures .…”

Section: Resultsmentioning

confidence: 99%

Process Optimisation Studies and Aminonitrile Substrate Evaluation of Rhodococcus erythropolis SET1, A Nitrile Hydrolyzing Bacterium

et al. 2020

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A comprehensive series of optimization studies including pH, solvent and temperature were completed on the nitrile hydrolyzing Rhodococcus erythropolis bacterium SET1 with the substrate 3-hydroxybutyronitrile. These identified temperature of 25°C and pH of 7 as the best conditions to retain enantioselectivity and activity. The effect of the addition of organic solvents to the biotransformation mixture was also determined. The results of the study suggested that SET1 is suitable for use in selected organo-aqueous media at specific ratios only. The functional group tolerance of the isolate with unprotected and protected β-aminonitriles, structural analogues of β-hydroxynitriles was also investigated with disappointingly poor isolated yields and selectivity obtained. The isolate was further evaluated with the αaminonitrile phenylglycinonitrile generating acid in excellent yield and ee (> 99 % (S) -isomer and 50 % yield). A series of pH studies with this substrate indicated pH 7 to be the optimum pH to avoid product and substrate degradation.

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“…High substrate concentrations, biocatalyst stability, and reuse through immobilization strategies provide driving forces towards more efficient productivity. Moreover, the combined use of organic solvents and immobilized biocatalysts, including the selection of an appropriate medium, could be applied to this biotransformation technique and improve the yield of 5‐CVAM 16, 17…”

Section: Resultsmentioning

confidence: 99%

Highly efficient synthesis of 5‐cyanovaleramide by Rhodococcus ruber CGMCC3090 resting cells

Shen

Zhang

et al. 2012

J of Chemical Tech & Biotech

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Biotransformation of nitriles using the solvent-tolerant nitrile hydratase from Rhodopseudomonas palustris CGA009

Cited by 19 publications

References 8 publications

Substrate Profiling of the Cobalt Nitrile Hydratase from Rhodococcus rhodochrous ATCC BAA 870

Substrate Profiling of the Cobalt Nitrile Hydratase from Rhodococcus rhodochrous ATCC BAA 870

Process Optimisation Studies and Aminonitrile Substrate Evaluation of Rhodococcus erythropolis SET1, A Nitrile Hydrolyzing Bacterium

Highly efficient synthesis of 5‐cyanovaleramide by Rhodococcus ruber CGMCC3090 resting cells

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