Nitrilase-catalysed conversion of acrylonitrile by free and immobilized cells of Streptomyces sp.

Nigam, Vinod Kumar; Khandelwal, Ankur; Gothwal, Raj Kumar; Mohan, M. Krishna; Choudhury, Bijan; Vidyarthi, Ambarish Sharan; Ghosh, Purnendu

doi:10.1007/s12038-009-0005-7

Cited by 42 publications

(25 citation statements)

References 23 publications

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“…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%

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: Introductionmentioning

confidence: 99%

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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“…Synthetic gels, on the contrary, have better mechanical properties, but mostly lower substrates and product diffusion coefficients [Leenen et al, 1996]. To date, there have been few reports about immobilization of nitrilase-producing bacteria employing chitosan , agar [Nigam et al, 2009], alginate [Chen et al, 2008;Shen et al, 2009], silica [Swartz et al, 2009], silica-carrageenan [Kabaivanova et al, 2011], glutaraldehyde [He et al, 2010], polyacrylamide and polyvinyl alcohol (PVA) [Vejvoda et al, 2006] as matrices. Though the gel beads of photo-crosslinked PVA and calcium-alginate mixtures have been applied successfully as carriers in a denitrification process [Dhake et al, 2011;Wang et al, 2007], there are no studies about using multiple polymers for immobilization of recombinant cells harboring nitrilase [Bryaskova et al, 2010].…”

Section: Introductionmentioning

confidence: 99%

Biosynthesis of Iminodiacetic Acid from Iminodiacetonitrile by Immobilized Recombinant <i>Escherichia coli</i> Harboring Nitrilase

et al. 2012

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Iminodiacetic acid (IDA) is widely used as an intermediate in the manufacture of chelating agents, glyphosate herbicides and surfactants. In the current work, the fragment with the length of 1,110 bp encoding the Acidovorax facilis nitrilase was obtained. The recombinant nitrilase expressed in Escherichia coli BL21 (DE3) was successfully used in the production of IDA from iminodiacetonitrile. To improve the stability of operation, the recombinant cells were entrapped in polyvinyl alcohol (PVA) and sodium alginate (SA) copolymer. The maximum relative nitrilase activity with 98.1% was further observed at 1.0% SA, 8.0% PVA, 1.0% CaCl₂, and 5.0% wet cells, under conditions of 1.0% iminodiacetonitrile in distilled water and a temperature of 40°C, respectively. The entrapped cells facilitated easy separation and good recycling compared with free cells. Moreover, the immobilized cells showed good operation and storage stability. This report is the first to describe IDA preparation using immobilized recombinant E. coli harboring nitrilase.

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“…Unlike structural complexity in natural urease, structure of urease construct obtained from this study has only 3 helices and 6 turns, it is assumed to confer its catalytic functions on urea-related compounds (aminourea and acrylamide). Nitrilases that hydrolyse organic nitriles to carboxylic acids and ammonia are a commercially interesting group of enzymes, as nitriles are important intermediates in the chemical synthesis of various products [30]. Nitrile-converting biocatalysts have considerable industrial interest as they can be used to treat toxic nitrile-and cyanide-containing wastes, and as agents for the synthesis of chemicals that have widespread applications [30][31][32][33].…”

Section: Discussionmentioning

confidence: 99%

“…Nitrilases that hydrolyse organic nitriles to carboxylic acids and ammonia are a commercially interesting group of enzymes, as nitriles are important intermediates in the chemical synthesis of various products [30]. Nitrile-converting biocatalysts have considerable industrial interest as they can be used to treat toxic nitrile-and cyanide-containing wastes, and as agents for the synthesis of chemicals that have widespread applications [30][31][32][33]. Urease conductometric biosensors are used for a quantitative estimation of general water pollution with heavy-metal ions [34].…”

Section: Discussionmentioning

confidence: 99%

Implication of Molecular Conservation on Computational Designing of Haloarchaean Urease with Novel Functional Diversity

Chellapandi¹,

Balachandramohan²

2012

Turk J Bioch

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Objective: The objective was to design an enzyme construct with diverse function from urease sequences of haloarchaean, Haloarcula marismortui ATCC 43049 based on its conserved domain consisting metal-binding region and active sites. Methods: Complete urease sequences of haloarchaea were retrieved from National Center for Biotechnology Information and then homology models generated, and validated. The best protein models were selected for docking with respective substrates using Ligand Fit program. The lowest energetic conformers were generated from these protein models by molecular dynamics methods. Urease construct-substrate complex was chosen based on the mode of catalysis, types of molecular interactions, and binding energy. Results:The resulted construct has a monomeric structure consisting of 3 helixes and 6 turns with 97 amino acids in length. The side chains of Asp49, Gly50 and Gln51 were predicted as functional residues in this construct. Urease construct was predicted to show catalytic function as similar to aliphatic nitrile hydradase and acrylamide hydro-lyase. Binding affinity of construct was more significant, which was better than to native urease. Urease construct was showed high binding affinity with semicarbazide and acrylamide wherein it has formed favorable hydrogen bonds. Conclusion: Substrate-binding region and active sites in the conserved domain of haloarchaean ureases are evolutionarily conserved at sequence as well as structural level. Substrate docking study supports the strong molecular interactions between construct and relative substrates. Thus, the present approach provides an insight to design urease construct with diverged catalytic function. Key Words: Molecular docking, urease, nitrilase, molecular evolution, enzyme design, haloarchaea Conflict of interest: Authors have no conflict of interest. ÖZETAmaç: Bu çalışmada, Haloarcula marismortui ATCC 43049'in metal bağlayan bölge ve aktif bölge gibi korunmuş domainleri esas alınarak haloarchaeanın üreaz dizilimine ters fonksiyonlu enzim yapısının tasarlanması amaçlandı. Yöntem: Haloarchaea ait üreaz dizisi, Ulusal Biyoteknoloji Bilgi Merkezinden alındı ve homolog modeller geliştirilerek doğrulama yapıldı. Docking için en uygun protein modelleri Ligand Fit programı kullanılarak ilgili substratlar ile seçildi. Bu protein modellerinden en düşük enerjili olan uyumlu modeller moleküler dinamik metodlar ile oluşturuldu. Üreaz yapı-substrat kompleks modeli enerji bağlama kapasitesi, moleküler etkileşim tipleri ve kataliz tipi esas alınarak seçildi. Bulgular: Meydana getirilen yapı 97 amino asit uzunluğunda 3 heliks ve 6 dönüş içeren monomer özelliğindedir. Bu yapıda Asp49, Gly50 ve Gln51 yan zincirleri fonksiyonel kalıntılar olarak öngörüldü. Üreaz yapısının ise alifatik nitril hidrataz ve akrilamid hidroliyaza benzer katalitik fonksiyonları olduğu düşünüldü. Oluşturulan üreazın bağlanma eğilimi esas üreazdan daha iyi olarak anlamlıydı. Ayrıca üreaz semikarbazid ve akrilamid ile yüksek bağlanma eğilimi gösterdi ve uygun hidrojen ba...

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Nitrilase-catalysed conversion of acrylonitrile by free and immobilized cells of Streptomyces sp.

Cited by 42 publications

References 23 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

Biosynthesis of Iminodiacetic Acid from Iminodiacetonitrile by Immobilized Recombinant <i>Escherichia coli</i> Harboring Nitrilase

Implication of Molecular Conservation on Computational Designing of Haloarchaean Urease with Novel Functional Diversity

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