Chemoenzymatic synthesis of d(−)phenylglycine using hydantoinase of Pseudomonas desmolyticum resting cells

Gokhale, D. V.; Bastawde, K. B.; Patil, S.G.; Kalkote, Uttam R.; Joshi, Rohini R.; Joshi, Ramesh A.; Ravindranathan, T.; Gaikwad, Bhaskar G.; Jogdand, V. V.; Nene, Sanjay

doi:10.1016/0141-0229(95)00127-1

Cited by 34 publications

(6 citation statements)

References 12 publications

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“…The reasons for these results may be that none of the strains possesses a carbamoylase gene or that the gene is not expressed or that the carbamoylase has no activity towards the two tested substrates. Similar results were also reported by Gokhale et al (1996) for three Pseudomonas strains. These bacteria showed hydantoinase activity towards PheHyd, but no carbamoylase activity towards the further hydrolysis of the produced NCPheGly was detected.…”

Section: Carbamoylase Activitysupporting

confidence: 93%

Stereoselective hydrolysis of aryl-substituted dihydropyrimidines by hydantoinases

Engel

Syldatk

Rudat

2011

Appl Microbiol Biotechnol

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In this study, we investigated the possibility of using a modified hydantoinase process for the production of optically pure β-amino acids. Two aryl-substituted dihydropyrimidines D,L-6-phenyl-5,6-dihydrouracil (PheDU) and para-chloro-D,L-6-phenyl-5,6-dihydrouracil (pClPheDU) were synthesized. Hydrolysis of these novel substrates to the corresponding N-carbamoyl-β-amino acids by three recombinant D-hydantoinases and several bacterial strains was tested. All applied recombinant D-hydantoinases and eight bacterial isolates catalyzed the conversion of PheDU to N-carbamoyl-β-phenylalanine (NCβPhe). Some of these biocatalysts showed an enantioselectivity for either the D- or the L-PheDU enantiomer. The second dihydropyrimidinase substrate pClPheDU was hydrolyzed by all three recombinant D-hydantoinases and six of the wild-type strains. To our knowledge, this is the first dihydropyrimidinase activity reported with this aryl-substituted dihydropyrimidine. For selected biocatalysts, hydantoinase activity towards aryl-substituted hydantoins was demonstrated as well. However, none of the bacterial strains tested so far exhibited any carbamoylase activity towards NCβPhe.

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Section: Carbamoylase Activitysupporting

confidence: 93%

Stereoselective hydrolysis of aryl-substituted dihydropyrimidines by hydantoinases

Engel

Syldatk

Rudat

2011

Appl Microbiol Biotechnol

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“…3.5.2.2). Second, either a chemical method (Takahashi et al, 1979; Gokhale et al, 1996) or an enzymatic route enables the subsequent hydrolysis of CpHPG to D-HPG. However, the enzymatic method, mediated by N-carbamoyl-D-amino acid amidohydrolase (hereinafter, carbamoylase), appears to be more appealing because the hydrolysis reaction can be conducted under milder conditions.…”

Section: Introductionmentioning

confidence: 99%

One-Step Production of D-p-Hydroxyphenylglycine by Recombinant Escherichia coli Strains

Chao

Lo³

et al. 1999

Biotechnol. Prog.

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The gene encoding D-hydantoinase from Agrobacterium radiobacter NRRL B11291 was successfully cloned by use of polymerase chain reaction. A positive clone was scored, and its nucleotide sequence was further analyzed. The analysis by deleting various lengths of nucleotides from the amino terminus of the open reading frame revealed the putative regions for promoter and RBS site. By highly expressing both D-hydantoinase and carbamoylase, recombinant Escherichia coli strains were able to convert DL-hydroxyphenyl hydantoin (DL-HPH) to D-p-hydroxyphenylglycine (D-HPG) with a conversion yield of 97%, accounting for productivity 5 times higher than that obtained by A. radiobacter NRRL B11291. Immobilizing the recombinant cells with kappa-carrageenan could also achieve a conversion of 93%, while A. radiobacter NRRL B11291 attained 20% within the same period of reaction time. These results illustrate the feasibility in employing recombinant E. coli to accomplish one-step conversion of DL-HPH to D-HPG. In the process of improving D-HPG production, D-hydantoinase activity was increased 2.57-fold but carbamoylase activity remained constant, which resulted in only a 30% increase in the reaction rate. It suggests that carbamoylase is the step setting the pace of the reaction. Since the reaction substrate is highly insoluble, achieving sufficient agitation appears to be an important issue in this heterogeneous system. This view is further supported by the study on repeated use of cells, which shows that to reach a conversion of more than 90% free cells can be recycled six times, whereas immobilized cells can be used only twice. In conclusion, the poor reusability of immobilized cells is due to the fouling on the gel surface.

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“…Chemoenzymatic synthesis of l ‐PG with the hydantoinase of Pseudomonas desmolyticum resting cells was carried out by Gokhale et al This pure product was further chemically converted to d (−)‐phenylglycine with nitrous acid with an 80% chemical yield. Thus, the overall conversion efficiency of d −5‐phenylhydantoin to d (−)‐phenylglycine was found to be 65–68%.…”

Section: Resultsmentioning

confidence: 99%

Synthesis and characterization of s‐histidine‐derived poly (ionic liquid)/silica nanocomposites and their application in the enantioselective hydrolysis of a chiral ester

Kowsari

Hosseini

Bakhshandeh

et al. 2013

J of Applied Polymer Sci

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In this study, a new optically active monomer containing two chemically preformed imide rings was synthesized. The monomer was then used to synthesize optically active poly(amide imide)s (OAPAIs) and an optically active polyionic liquid (OAPIL), which were finally reacted with various amounts of silica nanoparticles in an in situ polymerization reaction to produce OAPAI/SiO 2 and OAPIL/SiO 2 hybrid materials containing sulfonic acid groups. The prepared monomers and the OAPAI and OAPIL nanocomposites were characterized by 1 H-NMR spectroscopy, Fourier transform infrared spectroscopy, thermogravimetric analysis, X-ray diffraction, scanning electron microscopy, X-ray photoelectron spectroscopy, and differential scanning calorimetry. OAPIL/SiO 2 served as an excellent catalyst in water as a solvent for the hydrolysis of D,L-phenylglycine methyl ester with the advantage of a markedly enhanced enantioselectivity and activity. Also, the enantioselectivity was strongly dependent on the SiO 2 content in the OAPIL/SiO 2 systems; a favorable SiO 2 content was 20% (w/w). The enantioselectivity was 95.2% (substrate conversion 5 62.3%). V C 2013 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2014, 131, 39595.

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Chemoenzymatic synthesis of d(−)phenylglycine using hydantoinase of Pseudomonas desmolyticum resting cells

Cited by 34 publications

References 12 publications

Stereoselective hydrolysis of aryl-substituted dihydropyrimidines by hydantoinases

Stereoselective hydrolysis of aryl-substituted dihydropyrimidines by hydantoinases

One-Step Production of D-p-Hydroxyphenylglycine by Recombinant Escherichia coli Strains

Synthesis and characterization of s‐histidine‐derived poly (ionic liquid)/silica nanocomposites and their application in the enantioselective hydrolysis of a chiral ester

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