N-Carbamyl-<scp>L</scp>-Amino Acid Amidohydrolase ofPseudomonassp. Strain NS671: Purification and Some Properties of the Enzyme Expressed inEscherichia coli

Ishikawa, Takahiro; Watabe, Ken; Mukohara, Yukuo; Nakamura, Hiroaki

doi:10.1271/bbb.60.612

Cited by 20 publications

(19 citation statements)

References 5 publications

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“…Thermostabilization of proteins after immobilization was also reported earlier [42]. l-Hydantoinase and carbamoylase activities are reported to remain constant at the maximum level in the range of [45][46][47][48][49][50][51][52][53][54][55][56][57][58][59][60] • C [32]. The soluble d-hydantoinase lost 60% activity in 10 Min when the reaction was conducted at 70…”

Section: Figsupporting

confidence: 69%

Enhanced stability of newly isolated trimeric l‐methionine‐N‐carbamoylase from Brevibacillus reuszeri HSN1 by covalent immobilization

Nandanwar

Vohra

Hoondal

2013

Biotech and App Biochem

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Newly isolated and partially purified trimeric l-methionine-N-carbamoylase from Brevibacillus reuszeri HSN1 was immobilized by covalent coupling to a well-known support material, Eupergit® C. Approximately 80% enzyme activity yield was achieved with ≈61% binding of a soluble protein from a solution containing 5 mg/mL protein. The immobilized preparation was found to be quite unstable due to a poor multisubunit covalent interaction of trimeric enzyme. Additional cross-linking with polyaldehyde-dextran was done to sustain the biotechnological application of immobilized enzyme. The temperature and pH optima of immobilized enzyme were increased by 10°C and 0.5 unit, respectively. The enzyme was significantly stabilized and retained ≈93% enzyme activity when incubated at 60°C for 60 Min, whereas free enzyme lost ≈50% activity. It was recycled nine times with ≈100% conversion efficiency when batch experiments were carried out at 35°C, pH 7.5, for the 180 Min cycle, using 5% N-carbamoyl-l-methionine as the substrate. The half-life of the immobilized preparation was determined as 23 cycles and is significant. Approximately 50% of enzyme activity was retained even after 5 months of storage at 4°C, whereas free enzyme lost complete enzyme activity. Hence, we could enhance the stability of l-methionine-N-carbamoylase to make it a potential biocatalyst for biotechnological production of α-amino acids.

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Section: Figsupporting

confidence: 69%

Enhanced stability of newly isolated trimeric l‐methionine‐N‐carbamoylase from Brevibacillus reuszeri HSN1 by covalent immobilization

Nandanwar

Vohra

Hoondal

2013

Biotech and App Biochem

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“…The final reaction products (hydroxamic acids) are known to produce high chelating properties. Some of them (particularly α‐aminohydroxamic acid derivatives) are effective inhibitors of matrix metalloproteases, a family of zinc endopeptidases involved in tissue remodeling . Others (predominantly α‐aminohydroxamic acids, synthetic siderophores, acetohydroxamic acids, etc.)…”

Section: Biotechnological and Industrial Applicationsmentioning

confidence: 99%

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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“…18,22,23) Several microorganisms producing N-carbamoyl-D-and W or N-carbamoyl-Lamino acid amidohydrolases have been isolated, and some of these enzymes were puriˆed and characterized. 16,19,21,[24][25][26] These results suggest that there are 2 classes of N-carbamoyl amino acid amidohydrolases, N-carbamoyl-D-and N-carbamoyl-L-amino acid amidohydrolases. NCC amidohydrolase hydrolyzed only the L-form of NCC, 5) and showed signiˆcant similarity to the known N-carbamoyl-L-amino acid amidohydrolases (Fig.…”

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confidence: 83%

Identification, Cloning, and Sequencing of the Genes Involved in the Conversion ofD,L-2-Amino-Δ²-Thiazoline-4-Carboxylic Acid to …

Ohmachi¹,

Nishino²,

Kawata³

et al. 2002

Bioscience, Biotechnology, and Biochemistry

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N-Carbamyl-L-Amino Acid Amidohydrolase ofPseudomonassp. Strain NS671: Purification and Some Properties of the Enzyme Expressed inEscherichia coli

Cited by 20 publications

References 5 publications

Enhanced stability of newly isolated trimeric l‐methionine‐N‐carbamoylase from Brevibacillus reuszeri HSN1 by covalent immobilization

Enhanced stability of newly isolated trimeric l‐methionine‐N‐carbamoylase from Brevibacillus reuszeri HSN1 by covalent immobilization

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

Identification, Cloning, and Sequencing of the Genes Involved in the Conversion ofD,L-2-Amino-Δ²-Thiazoline-4-Carboxylic Acid to …

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N-Carbamyl-L-Amino Acid Amidohydrolase ofPseudomonassp. Strain NS671: Purification and Some Properties of the Enzyme Expressed inEscherichia coli

Cited by 20 publications

References 5 publications

Enhanced stability of newly isolated trimeric l‐methionine‐N‐carbamoylase from Brevibacillus reuszeri HSN1 by covalent immobilization

Enhanced stability of newly isolated trimeric l‐methionine‐N‐carbamoylase from Brevibacillus reuszeri HSN1 by covalent immobilization

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

Identification, Cloning, and Sequencing of the Genes Involved in the Conversion ofD,L-2-Amino-Δ2-Thiazoline-4-Carboxylic Acid to …

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Product

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Identification, Cloning, and Sequencing of the Genes Involved in the Conversion ofD,L-2-Amino-Δ²-Thiazoline-4-Carboxylic Acid to …