Nitrilase mediated conversion of Indole-3-acetonitrile to Indole-3-acetic acid

Agarwal, Ankur; Nigam, Vinod Kumar

doi:10.1016/j.bcab.2014.05.005

Cited by 12 publications

(7 citation statements)

References 31 publications

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“…The activity of nitrilase was studied at 60°C for 1 h in a 1.0 mL reaction mixture that contained phosphate buffer, 2 mM of IAN and the whole cells (*0.0010 g dry cell weight, DCW). The enzyme substrate reaction was stopped by adding 0.05 mL, 2 N HCl [8]. The reaction mixture was centrifuged at 10,000 rpm for 10 min at 4°C.…”

Section: Nitrilase Assaymentioning

confidence: 99%

“…MTCC 7546 was reported to produce thermostable, broad spectrum nitrilase catalyzing both mono and dinitriles. It can also hydrolyze IAN at 60°C in a single step pathway without formation of amide as intermediate [4,8]. Therefore, an increased production of such eco-friendly biocatalyst will be of utmost importance.…”

Section: Introductionmentioning

confidence: 99%

“…Nitrilase carry out reactions in mild and environmental friendly conditions. They are used for bioconversion of various nitriles to commercially important chemicals such as acrylic acid, methacrylic acid, p-methoxy phenylacetic acid, nicotinic acid and indole-3-acetic acid (IAA) [3][4][5][6][7][8][9]. Rhizobium, Agrobacterium tumefaciens, a few Bradyrhizobium sp.…”

Section: Introductionmentioning

confidence: 99%

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Enhanced Production of Nitrilase from Streptomyces sp. MTCC 7546 by Response Surface Method

Agarwal

Nigam

2015

Proc. Natl. Acad. Sci., India, Sect. B Biol. Sci.

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Nitrilases are enzymes with varied applications preferably used in preparation of industrially important compounds as well as in bioremediation processes. The production of enzymes is influenced by medium compositions as some of the constituents of medium directly affect the enzyme synthesis. In the present study, the components of the medium are optimized by classical and response surface methodology to maximize the production of intracellular nitrilase from Streptomyces sp. MTCC 7546. Glucose was observed as the most suitable carbon source for production of nitrilase by 'one factor at a time'. The optimal concentration of glucose (5 g/L) was set as zero coded level for further optimization study. A central composite design was employed to study the effect of interaction among glucose, yeast extract and mineral base and evaluated for maximum nitrilase yield. The nitrilase production of 11.54 U/mg was observed at 24 h in medium containing 6.5 g/L glucose, 1.0 g/L yeast extract and 220 mL/L mineral base with 10 mM of benzonitrile as inducer. A twofold increment from 5.95 U/mg in the enzyme yield was observed after the optimization study of response surface methodology.

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Section: Nitrilase Assaymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Enhanced Production of Nitrilase from Streptomyces sp. MTCC 7546 by Response Surface Method

Agarwal

Nigam

2015

Proc. Natl. Acad. Sci., India, Sect. B Biol. Sci.

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“…(Rezende et al 2004), Kluyveromyces thermotolerans (Prasad et al 2005), Streptomyces sp. MTCC7546 (Agarwal and Nigam, 2014), Geobacillus pallidus (Makhongela et al 2007), and Rhodococcus sp. (Chand et al 2004;Reisinger et al 2004;Choia et al 2008;Ma et al 2010;Dong et al 2011).…”

Section: Introductionmentioning

confidence: 99%

Nitrile-metabolizing potential ofBacilluscereus strain FA12; Nitrilase production, purification, and characterization

Ramezani-pour

Badoei-dalfard

Namaki-Shoushtari

et al. 2015

Biocatalysis and Biotransformation

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Nitrile-hydrolyzing bacteria have the potential to perform useful biotransformations such as the production of industrially useful acids and amides. In this study, we report a nitrile-degrading bacterium with signifi cant nitrile metabolism. Molecular characterization of 16S rDNA gene characterized this strain as Bacillus cereus . Medium optimization of B. cereus FA12 showed that biomass and nitrilase production was strongly supported by glucose (10 gL Ϫ 1 ) and yeast extract (10 gL Ϫ 1 ). Enzymatic production improved slightly in the pH range from 6.0 to 7.0. The addition of Mg ϩ 2 , Fe ϩ 2 , and Na ϩ supported biomass and nitrilase production; however, other metal ions, Co ϩ 2 and Cu ϩ 2 , inhibited production. The apparent molecular mass of the puri fi ed FA12 nitrilase as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was about 45 kDa. Nitrilase FA12 shows relatively high activity and stability at pH 7.0 and 40 ° C. Nitrilase FA12 was marginally inhibited with Ca ϩ 2 and Co ϩ 2 , whereas inhibition in the presence of dithiothreitol or DTT was 80%. The pseudo K m (mM) values of resting cells (i.e., treating whole cells as if they were an enzyme) for acetonitrile and acetamide were determined to be 2.36 and 1.81, respectively. Under optimum situations, B. cereus FA12 resting cells produced 83 and 58 (U/mg) acetonitrile/acetamide degrading activity, respectively. Ammonia production from acetamide and acetonitrile by the B. cereus FA12 was maximum after 5 and 7 h of incubation, respectively. These results indicate that B. cereus FA12 resting cells may be used in nitrile biotransformations to produce commercially useful compounds.

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“…Therefore, due to their wider applicability in different perspective, they are considered as "Green Catalyst 8,9 . 3-cyanopyridine is a nitrile compound which hydrolyses into nicotinic acid (also known as vitamin B 3 , niacin or vitamin PP) and ammonia in presence of 3-cyanopyridinase enzyme, a type of nitrilase enzyme 10,11,12 . Niacin is associated with a pandemic deficiency disease known as pellagra.…”

Section: Fig 1: the Representation Of Two Pathways Involved In The Dmentioning

confidence: 99%

Untitled

2017

IJPSR

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A thermostable bacterial 3-cyanopyridinase enzyme has been identified that catalyze 3-cyanopyridine to nicotinic acid and ammonia. Nicotinic acid is mainly used in food, pharmaceutical and biochemical industries. This study was undertaken to optimize the purification of 3-cyanopyridinase enzyme and characterization of its various kinetic properties. The partial purification of enzyme has been carried out in five steps that results in approximately 2.3 fold increased purification with 46.5 % of enzyme recovery. The partially purified enzyme was observed approximately 43 kDa of maximum activity at 50 °C temperature and pH 7.0. The partially purified enzyme showed the K m of 0.91 mM and maximum velocity (V max ) of 0.59 U. The half-life (t 1/2 ) of partially purified enzyme was about 60 min at optimal conditions. The enzyme has broad substrate specificity, hydrolyzing toxic compounds such as benzonitrile and propionitrile. Thus this novel enzyme has potential in bioremediation process.

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Nitrilase mediated conversion of Indole-3-acetonitrile to Indole-3-acetic acid

Cited by 12 publications

References 31 publications

Enhanced Production of Nitrilase from Streptomyces sp. MTCC 7546 by Response Surface Method

Enhanced Production of Nitrilase from Streptomyces sp. MTCC 7546 by Response Surface Method

Nitrile-metabolizing potential ofBacilluscereus strain FA12; Nitrilase production, purification, and characterization

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