Novel direct synthesis of l-phenylalanine methyl ester by using Rhodotorula glutinis phenylalanine ammonia lyase in an organic-aqueous biphasic system

D’Cunha, Godwin B.; Satyanarayan, Vaduvatha; Nair, P.M.

doi:10.1016/0141-0229(94)90173-2

Cited by 28 publications

(26 citation statements)

References 18 publications

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“…Use of phenylalanine ammonia lyase (E.C.4.3.1.5, PAL), which catalyzes the spontaneous, non‐oxidative deamination of L‐phenylalanine (L‐Phe) to trans ‐cinnamic acid ( t ‐CA)6 according to the equation shown below, has received increased attention in the synthesis of L‐Phe7–9 and L‐phenylalanine methyl ester (L‐PM)10, 11 because of the low price of substrates, t ‐CA and trans ‐cinnamyl methyl ester ( t ‐CM) 7–11 PAL, a tetramer, is widely distributed and is well characterized from plant and microbial sources 6–11. In addition to the use of the enzyme in the synthesis of L‐Phe and L‐PM, it has been used extensively for clinical applications 12, 13…”

Section: Introductionmentioning

confidence: 99%

“…We have previously reported methods for the direct one‐step synthesis of L‐PM (a precursor of the artificial sweetener, aspartame) in an organic‐aqueous biphasic system using PAL containing Rhodotorula glutinis yeast whole cells10, 11; and isolation of PAL in pure form 14. In this study, our focus is on the investigation of how OS interactions affect purified PAL activity.…”

Section: Introductionmentioning

confidence: 99%

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Enzyme activity evaluation of organic solvent‐treated phenylalanine ammonia lyase

Quinn

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D’Cunha

2011

Biotechnology Progress

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The direct one-step synthesis of L-phenylalanine methyl ester in an organic-aqueous biphasic system using phenylalanine ammonia lyase (E.C.4.3.1.5, PAL) containing Rhodotorula glutinis yeast whole cells was reported earlier. We report here further optimization of this biotransformation using isolated PAL, when the lyophilized enzyme is treated with different water miscible and water immiscible organic solvents. Use of isolated PAL enzyme is advantageous in overcoming diffusion barriers encountered when using PAL containing R.glutinis whole cells, and resulted in increased product yield due to better interaction of enzyme with the substrate. Among the water miscible solvents, ethanol treated and methanol-treated enzymes supported maximum PAL forward and reverse activities; respectively. In the water immiscible solvents category, heptane-treated enzyme exhibited maximal activity for both PAL forward and reverse reactions. PAL activity obtained with enzyme specimens treated with methanol, ethanol, and heptane varied in the range of 91–99% of that observed in aqueous buffer medium for the forward reaction; and 89–95% for the reverse reaction. n-butanol,acetone, and benzene were found to have a inhibitory effect on PAL enzyme, in that, it resulted in only 31–33% activity of that obtained with aqueous solution. Raman spectroscopy was used to monitor amide I and II bands which are sensitive to changes in the secondary structure of proteins. No changes in structure could be detected from the analyses of AI and AII bands of PAL spectra. This data obtained for PAL, a tetramer, could be significant in predicting how solvent interactions affect the structure and function of multimeric proteins and enzymes in nonaqueous media.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Enzyme activity evaluation of organic solvent‐treated phenylalanine ammonia lyase

Quinn

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D’Cunha

2011

Biotechnology Progress

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“…PAL ist für L ‐Phenylalanin spezifisch, jedoch wird auch L ‐Tyrosin in geringerem Maße als Substrat akzeptiert 59. PAL‐Enzyme wurden genutzt, um unterschiedliche Phenylring‐substituierte, polycyclisch‐aromatische sowie heterocyclische L ‐Arylalanine sowie den L ‐Phenylalaninmethylester durch Addition von Ammoniak an die entsprechende Doppelbindung umzusetzen 93…”

Section: Enzyme Zur Herstellung Chiraler Amine Und Aminosäurenunclassified

Biokatalysatoren für die organische Synthese – die neue Generation

et al. 2014

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Die Verwendung von Enzymen als Katalysatoren zur Synthese neuartiger Verbindungen ist in den letzten Jahren zunehmend in den Fokus gerückt. Entsprechend hohe Erwartungen werden an die Entdeckung und Identifizierung neuer Biokatalysatoren für die organische Synthese gestellt. Dies spiegelt sich auch in der Komplexität der adressierten Reaktionen wider. Der Anwendungsbereich von Biokatalysatoren umfasst die Synthese wichtiger Zwischenprodukte für die pharmazeutische und chemische Industrie sowie die Entwicklung neuer enzymatischer Techniken und Prozesse. Enzyme sind ein wichtiger Teil des Spektrums an Katalysatoren, die der Synthesechemie zur Verfügung stehen. Die Vorteile und Anwendungsmöglichkeiten der neuesten und höchst vielversprechenden Generation von Biokatalysatoren – Reduktasen, Transaminasen, Ammoniak‐Lyasen, Epoxidhydrolasen und Dehalogenasen – werden hier vorgestellt und anhand der Synthese von Schlüsselmolekülen beispielhaft diskutiert.

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“…4.3.1.11), is capable of synthesizing L-DOPA (23) from 3,4-dihydroxy-trans-caffeic acid (22), but this starting material is not as readily available as catechol, pyruvate, and ammonia are. 4.3.1.11), is capable of synthesizing L-DOPA (23) from 3,4-dihydroxy-trans-caffeic acid (22), but this starting material is not as readily available as catechol, pyruvate, and ammonia are.…”

Section: Histidine Ammonia Lyasementioning

confidence: 99%

Addition of Amines to C = C Bonds

Wubbolts¹

2002

Enzyme Catalysis in Organic Synthesis

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Novel direct synthesis of l-phenylalanine methyl ester by using Rhodotorula glutinis phenylalanine ammonia lyase in an organic-aqueous biphasic system

Cited by 28 publications

References 18 publications

Enzyme activity evaluation of organic solvent‐treated phenylalanine ammonia lyase

Enzyme activity evaluation of organic solvent‐treated phenylalanine ammonia lyase

Biokatalysatoren für die organische Synthese – die neue Generation

Addition of Amines to C = C Bonds

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