A novel Pseudomonas putida strain with high levels of hydantoin-converting activity, producing l-amino acids

Buchanan, K.J.; Burton, Stephanie G.; Dorrington, Rosemary A.; Matcher, Gwynneth F.; Skepu, Zoleka

doi:10.1016/s1381-1177(00)00036-9

Cited by 17 publications

(6 citation statements)

References 24 publications

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“…The magnesium interacts with the oxygen of the triphosphate chain, thereby weakening the phosphorous-oxygen bond and making it more susceptible to cleavage reaction required for phosphoryl transfer. Buchanan et al [21] indicated the addition of MgSO 4 .7H 2 O resulted in an increase in hydantoinase activity. Our results was disagreed with Mandal and Mandal [22] they reported that magnesium enhanced biogas production from organic wastes for an optimum value of 45 mg for 300 cm − ³ slurry but the presence of magnesium inside the fermentation medium was better for bacterial growth not for biogass production and that was clear when it is added even small amount to the fermentation medium suggested that each bacterium species need selected requirements with selected concentration to produce such products with maximum productivity.…”

Section: Effect Of Calcium Additionmentioning

confidence: 99%

Trace Metal Effect on Hydrogen Production Using C.acetobutylicum

Alshiyab

Kalil²,

Hamid³

et al. 2008

OnLine J. of Biological Sciences

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This study was carried out to study the effect of trace metal addition for hydrogen production The results show that this bacterial need a selected nutrient with selected concentration. The optimum parameters for cultivation were at initial pH of 7.0 and temperature of 30°C. Trace metal addition to the new medium showed that only iron enhanced the H 2 yield. The results showed that 25 mgL −1 FeSO 4 ⋅7H 2 O enhanced the hydrogen yield from 391 mLg −1 to 408 mLg −1 glucose utilized with biomass concentration of 1.38 gL

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Section: Effect Of Calcium Additionmentioning

confidence: 99%

Trace Metal Effect on Hydrogen Production Using C.acetobutylicum

Alshiyab

Kalil²,

Hamid³

et al. 2008

OnLine J. of Biological Sciences

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“…This is the fi rst of many drugs as protease inhibitors for preventing HIV infection, peptide ligands for the fi brinogen receptor, effective tachykinin antagonists, and neuronal receptor ligands [Li et al, 1999]. N-carbamoyl-L -amino acid amidohydrolase ( L -Ncarbamoylase) enzyme has been found in several microorganisms of the genera Alcaligenes [Ogawa et al, 1995], Arthrobacter , Bacillus [Yamashiro et al, 1988], Flavobacterium [Yokozeki et al, 1987] and Pseudomonas [Buchanan et al, 2001]. Although its biological function is still unknown [Pietzsch and Syldatk, 2002], from the biotechnological point of view L -N-carbamoylase plays an important role in the production of optically pure L -amino acids by an enzymatic method named 'hydantoinase process' [Altenbuchner et al, 2001].…”

Section: Introductionmentioning

confidence: 99%

Molecular Cloning and Biochemical Characterization of <i>L</i>-N-Carbamoylase from <i>Sinorhizobium meliloti</i> CECT4114

et al. 2005

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An N-carbamoyl-L-amino acid amidohydrolase (L-N-carbamoylase) from Sinorhizobium meliloti CECT 4114 was cloned and expressed in Escherichia coli. The recombinant enzyme catalyzed the hydrolysis of N-carbamoyl α-amino acid to the corresponding free amino acid, and its purification has shown it to be strictly L-specific. The enzyme showed broad substrate specificity, and it is the first L-N-carbamoylase that hydrolyses N-carbamoyl-L-tryptophan as well as N-carbamoyl L-amino acids with aliphatic substituents. The apparent K_m values for N-carbamoyl-L-methionine and tryptophan were very similar (0.65 ± 0.09 and 0.69 ± 0.08 mM, respectively), although the rate constant was clearly higher for the L-methionine precursor (14.46 ± 0.30 s^–1) than the L-tryptophan one (0.15 ± 0.01 s^–1). The enzyme also hydrolyzed N-formyl-L-methionine (k_cat/K_m = 7.10 ± 2.52 s^–1·mM^–1) and N-acetyl-L-methionine (k_cat/K_m = 12.16 ± 1.93 s^–1·mM^–1), but the rate of hydrolysis was lower than for N-carbamoyl-L-methionine (k_cat/K_m = 21.09 ± 2.85). This is the first L-N-carbamoylase involved in the ‘hydantoinase process’ that has hydrolyzed N-carbamoyl-L-cysteine, though less efficiently than N-carbamoyl-L-methionine. The enzyme did not hydrolyze ureidosuccinic acid or 3-ureidopropionic acid. The native form of the enzyme was a homodimer with a molecular mass of 90 kDa. The optimum conditions for the enzyme were 60°C and pH 8.0. Enzyme activity required the presence of divalent metal ions such as Ni²⁺, Mn²⁺, Co²⁺ and Fe²⁺, and five amino acids putatively involved in the metal binding were found in the amino acid sequence.

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“…The results were different from the strains reported, such as only IMH caused a significant induction of hydantoinase activity in Arthrobacter sp. DSM3747 (Gross et al 1990) and Flavobacterium sp (Nishida et al 1987), while MSH caused induction of hydantoinase in Pseudomonas sp NS671 (Ishikawa et al 1993) and hydantoin caused induction of hydantoinase in Pseudomonas putida (Buchanan et al 2001). These properties indicate that the strain MH602 is a novel hydantoinase-producing microorganism.…”

Section: Effect Of Inducers On Enzyme Formationmentioning

confidence: 99%

“…According to the research reported to date, productivity and substrate specificity of the hydantoinase and carbamoylase from different bacterial sources vary considerably. Pseudomonas putida (Buchanan et al 2001) only yields aliphatic L-amino acids with the bioconversion yield of about 60% from corresponding DL-5-substituted hydantoins. Bacillus stearothermophilus NS1122A and Arthrobacter sp.…”

Section: Introductionmentioning

confidence: 99%

Enzymatic production of l-amino acids from the corresponding dl-5-substituted hydantoins by Bacillus fordii MH602

Mei

Ouyang

2007

World J Microbiol Biotechnol

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Bacillus fordii MH602 was newly screened from soil at 45°C and exhibited high activities of hydantoinase and carbamoylase, efficiently yielding L-amino acids including phenylalanine, phenylglycine and tryptophan with the bioconversion yield of 60-100% from the corresponding DL-5-substituted hydantoins. Hydantoinase activity was found to be cell-associated and inducible. The optimal inducer was DL-5-methylhydantoin with concentration of 0.014 mol L -1 and added to the fermentation medium in the exponential phase of growth. In the production of optically pure amino acids from DL-5-benylhydantoin, the optimal temperature and pH of this reaction were 45-50°C and 7.5 respectively. The hydantoinase was non-stereoselective, while carmbamoylase was L-selective. The hydantoinase activity was not subject to substrate inhibition, or product inhibition by ammonia. In addition, The activities of both enzymes from crude extract of the strain were thermostable; the hydantoinase and carbamoylase retained about 90% and 60% activity after 6 h at 50°C, respectively. Since reaction at higher temperature is advantageous for enhancement of solubility and for racemization of DL-5-substituted hydantoins, the relative paucity of L-selective hydantoinase systems, together with the high level of hydantoinase and carbamoylase activity and unusual substrate selectivity of the strain MH602, suggest that it has significant potential applications.

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A novel Pseudomonas putida strain with high levels of hydantoin-converting activity, producing l-amino acids

Cited by 17 publications

References 24 publications

Trace Metal Effect on Hydrogen Production Using C.acetobutylicum

Trace Metal Effect on Hydrogen Production Using C.acetobutylicum

Molecular Cloning and Biochemical Characterization of <i>L</i>-N-Carbamoylase from <i>Sinorhizobium meliloti</i> CECT4114

Enzymatic production of l-amino acids from the corresponding dl-5-substituted hydantoins by Bacillus fordii MH602

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