β-Lactamase-Free Penicillin Amidase from Alcaligenes sp.: Isolation Strategy, Strain Characteristics, and Enzyme Immobilization

Pal, A. K.; Samanta, Timir B.

doi:10.1007/s002849900453

Cited by 11 publications

(6 citation statements)

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“…Majority of amidase producing microorganisms exhibited optimum growth and production of enzyme around neutral pH (Pal and Samanta 1999;Ciskanik et al 1995) except amidases in Rhodococcus rhodochrous NHB-2 and Kluyveromyces thermotolerans MGBY 37 which have optimum pH 5.5-6.0 and 6.2, respectively (Bhalla et al 1997;Prasad et al 2005). Amidase from thermophiles are generally active over wide pH range (5-9.5) (Egorova et al 2004;Makhongela et al 2007).…”

Section: Physiochemical Characterization Of Amidasesmentioning

confidence: 96%

Amidases: versatile enzymes in nature

Sharma

Bhalla

2009

Rev Environ Sci Biotechnol

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Amidases are ubiquitous enzymes and biological functions of these enzymes vary widely. In past five decades, they turned out to be an attractive tool in industries for the synthesis of wide variety of carboxylic acids, hydroxamic acids and hydrazide, which find applications in commodity chemicals synthesis, pharmaceuticals agrochemicals and waste water treatments etc. Their proteins structures revealed that aliphatic amidases share the typical a/b hydrolase fold (like nitrilase superfamily) and signature amidases are evolutionary related to aspartic proteinases. They hydrolyse wide variety of amides (short chain aliphatic amides, mid-chain amides, arylamides, a-aminoamides and a-hydroxyamides) and can be grouped on the basis of their catalytic site and preferred substrate. They resist denaturation at extreme of pH and temperature because of their strong and compact multimeric structures. Inhibition studies and three-dimensional analysis of the structures identified a Glu59, Lys134, Cys166 catalytic triad and follow ''Bi-bi Ping-Pong'' mechanism reaction for amide hydrolysis and acyl transferase reactions. Many recombinant amidases have been expressed in Escherichia coli as well as in Brevibacterium lactofermentum.

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Section: Physiochemical Characterization Of Amidasesmentioning

confidence: 96%

Amidases: versatile enzymes in nature

Sharma

Bhalla

2009

Rev Environ Sci Biotechnol

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“…However, this organism efficiently produced biomass and acyl transfer activity around neutral pH (7.5). Most of amidase producing organism which exhibit acyl transfer activity grow and produce enzyme around neutral pH [11,12]. Alcaligenes sp.…”

Section: Discussionmentioning

confidence: 99%

Production and Characterization of Acyl Transfer Activity of Amidase from Alcaligenes sp. MTCC 10674 for Synthesis of Hydroxamic Acids

Kant¹

2013

J Microb Biochem Technol

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Alcaligenes sp. MTCC 10674 has been isolated as a nitrile degrading bacterium from the soil. Amidase of this organism exhibited dual activity i.e. hydrolase as well as acyl transfer. The acyl transfer activity of this organism has been used for the synthesis of variety of hydroxamic acids. Optimization of physiochemical parameters resulted into 30 folds increase in the acyl transfer activity of amidase (0.039 Umgdcm -1 to 1.17 Umgdcm -1 ). The acyl transfer activity of amidase of this organism has broader substrate affinity ranging from a variety of aliphatic amides (formamide, acetamide, propanamide etc.) to aromatic amides (benzamide, mandelamide, nicotinamide etc.) along with hydroxylamine for the biotransformation of these amides into corresponding hydroxamic acid. This enzyme is quite stable at 50°C with t 1/2 for 8h and at 60°C this amidase have t 1/2 for 1.30 h. The acyl transfer activity of amidase of Alcaligenes sp. MTCC 10674 under high temperature condition makes of potential application in developing a bioprocess for the production of variety of aliphatic and aromatic hydroxamic acid.

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“…JR1, acetonitrile has been reported to be a suitable carbon source (Rezende et al, 2004). In general, the ATA of amidase is produced constitutively by many microbes, whereas in some microorganisms it is induced by amides and nitriles (Pal and Samanta, 1999). The ATA of Pseudomonas putida BR-1 is also inducible in nature, and isobutyronitrile (0.3% v/v) proved to be the best inducer for the production of ATA.…”

Section: Discussionmentioning

confidence: 99%