A comparative study on the production of amidase using immobilized and dehydrated immobilized cells of Pseudomonas putida MTCC 6809

Chacko, Sonia; Ramteke, Pramod W.; Joseph, Babu

doi:10.1016/j.jgeb.2012.01.003

Cited by 10 publications

(7 citation statements)

References 35 publications

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“…The result concluded that P. putida AP-2 is a novel mesophilic bacterial strain that has ability to produce huge amount of amidase enzyme in short period of time in comparison to other microorganisms already described in the literature (Nampoothiri et al 2005;Wang et al 2008;Chacko et al 2012). The reported strain, P. putida AP-2, may be used for commercial production of amidase enzyme and the microbe having great potential in bioremediation as it is able to utilize heavy metals for their growth.…”

Section: Resultsmentioning

confidence: 83%

Production optimization of extracellular amidase enzyme by newly isolated Pseudomonas putida AP-2 from agricultural soil

Abada

2014

Rend. Fis. Acc. Lincei

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Amidases are ubiquitous enzymes that have received increased attention due to their wide range of biotechnological applications, especially in industries for the synthesis of wide variety of carboxylic and hydroxamic acids, which find applications in pharmaceuticals, agrochemicals and waste water treatments. In the present study, 40 bacterial isolates were screened for extracellular amidase-producing capability, and on the basis of color development, 5 isolates were selected for amidase production in broth media. Based on enzyme production, one of the most potent isolates identified as Pseudomonas putida AP-2 was selected for further study. The effects of media composition and various fermentation conditions for optimization of amidase production were studied. The maximum extracellular amidase production was obtained at 30°C and pH 8.0 after 36 h of incubation in shaking condition. Among the substrate, acetamide was the best; however, P. putida AP-2 also utilized acrylamide which is a known carcinogen. Regarding carbon sources, glucose was the best, while peptone was found the best nitrogen source. The isolated bacterium, P. putida AP-2, is also tolerant to number of heavy metals at higher levels so this may also be applied for field application in contaminated soil.

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Section: Resultsmentioning

confidence: 83%

Production optimization of extracellular amidase enzyme by newly isolated Pseudomonas putida AP-2 from agricultural soil

Abada

2014

Rend. Fis. Acc. Lincei

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“…Thanks to their broad substrate specificity and stereoselectivity, amidases have significant potential for employment as biocata lysts in organic synthesis [2,3]. These enzymes are particularly important for the synthesis of enantiomer ically pure amino acids, nonsteroidal anti inflamma tory drugs, and obtaining optically active 2 aryl pro pionic acids from corresponding racemic mixtures of amino acid amides [4]. They are also used for the pro duction of acrylic acid from acrylamide [4].…”

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confidence: 99%

“…These enzymes are particularly important for the synthesis of enantiomer ically pure amino acids, nonsteroidal anti inflamma tory drugs, and obtaining optically active 2 aryl pro pionic acids from corresponding racemic mixtures of amino acid amides [4]. They are also used for the pro duction of acrylic acid from acrylamide [4].…”

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confidence: 99%

“…Amidases typically operate in a narrow range of pH and temperature, which complicates their use in biocatalysis. In this regard, immobilization of microbial cells, which possess amidase activity, pro vides some advantage in resistance to adverse environ mental factors and toxic substances, as well as possibil ities for long term use of the biocatalyst in a continu ous process [4].…”

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confidence: 99%

“…Among these, cells of Delftia tsuruhatensis CCTCC M205114 encapsulated in calcium alginate have been reported to carry out enantiomer selective hydrolysis of (R) 2, 2 dimethyl cyclopropane carboxamide from a race mic mixture, resulting in the accumulation of S amide, which is a key intermediate in the synthesis of cilastatin [7]. Cells of Pseudomonas putida MTCC 6809, incorporated into the structure of calcium algi nate gel, were used for the production of amidase [4]. A membrane reactor was implemented for the produc tion of nicotinic acid from nicotinamide in a reaction catalyzed by amidase from Microbacterium imperial CBS 498-74 [8].…”

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confidence: 99%

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Transformation of amides by adherent Rhodococcus cells possessing amidase activity

Maksimova

Gorbunova

Зорина

et al. 2014

Appl Biochem Microbiol

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We report the development of a heterogeneous biocatalyst for the hydrolysis of amides that is based on cell adhesion of amidase containing Rhodococci on activated birch charcoal (ABC) and raw coal. We investigated the properties of the obtained biocatalyst in the hydrolysis reaction of acrylamide to acrylic acid and nicotinamide to nicotinic acid, as well as in a model reaction of racemic lactamide hydrolysis to a mixture of D and L isomers of lactic acid. We show that a six and threefold increase in the concentrations of adher ent and suspended cells, respectively, results in a reduction of amidase activity by 3 and 30 times, respectively. Cells adherent on ABC maintained more than 50% of enzymatic activity for seven 24 hour cycles of acryla mide hydrolysis, while suspended cells lost more than 60% of activity already in the second cycle. We also noted that cell adhesion on ABC reduced the stereoselectivity of hydrolysis reaction of racemic lactamide.

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Nitrile‐converting enzymes: An eco‐friendly tool for industrial biocatalysis

Ramteke

Maurice

Joseph

et al. 2013

Biotech and App Biochem

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Nitriles are organic compounds bearing a − C ≡ N group; they are frequently known to occur naturally in both fauna and flora and are also synthesized chemically. They have wide applicability in the fields of medicine, industry, and environmental monitoring. However, the majority of nitrile compounds are considered to be lethal, mutagenic, and carcinogenic in nature and are known to cause potential health problems such as nausea, bronchial irritation, respiratory distress, convulsions, coma, and skeletal deformities in humans. Nitrile-converting enzymes, which are extracted from microorganisms, are commonly termed nitrilases and have drawn the attention of researchers all over the world to combat the toxicity of nitrile compounds. The present review focuses on the utility of nitrile-converting enzymes, sources, classification, structure, properties, and applications, as well as the future perspective on nitrilases.

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A comparative study on the production of amidase using immobilized and dehydrated immobilized cells of Pseudomonas putida MTCC 6809

Cited by 10 publications

References 35 publications

Production optimization of extracellular amidase enzyme by newly isolated Pseudomonas putida AP-2 from agricultural soil

Production optimization of extracellular amidase enzyme by newly isolated Pseudomonas putida AP-2 from agricultural soil

Transformation of amides by adherent Rhodococcus cells possessing amidase activity

Nitrile‐converting enzymes: An eco‐friendly tool for industrial biocatalysis

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