Penicillin acylase-catalyzed resolution of amines in aqueous organic solvents

Langen, Luuk M. van; Oosthoek, N.H.P.; Guranda, D. T.; Rantwijk, Fred van; Švedas, Vytas K.; Sheldon, Roger A.

doi:10.1016/s0957-4166(00)00442-0

Cited by 62 publications

(34 citation statements)

References 29 publications

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“…Phenylacetylchloride (0.022 mol) was added dropwise to 50 ml NaOH solution (10%, w/v) of racemic tert-Leucine (0.02 mol) in an ice-water bath [17]. The reaction mixture was acidified to pH 2 with 6 M HCl and extracted with ethyl acetate followed by recrystallization.…”

Section: Standard Determination Of the Enzyme Activitymentioning

confidence: 99%

Effect of organic cosolvent on kinetic resolution of tert-leucine by penicillin G acylase from Kluyvera citrophila

Liu

Wei

Song

et al. 2005

Bioprocess Biosyst Eng

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Penicillin G acylase (PGA) from Kluyvera citrophila immobilized on Amberzyml was used for enantioselective hydrolysis of N-phenylacetylated-DL-tert-leucine (N-Phac-DL-Tle) to produce L-tert-leucine (L-Tle). The effects of various organic cosolvents on hydrolysis of N-Phac-DL-Tle have been investigated in aqueous-cosolvent medium. It was founded that the rate of PGA-catalyzed reaction was significantly affected by the presence of 2% (v/v) organic cosolvent concentration. The initial rate fell with increasing logP of the cosolvent, but for logP values less than -0.24 the rate was faster than in purely aqueous medium. Additionally, the relative rate increases with the increase of dielectric constant (epsilon) of organic cosolvents. The yields of L-Tle in all aqueous-cosolvent systems were above 95% with the enantiomeric excess (ee) of >99%.

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Section: Standard Determination Of the Enzyme Activitymentioning

confidence: 99%

Effect of organic cosolvent on kinetic resolution of tert-leucine by penicillin G acylase from Kluyvera citrophila

Liu

Wei

Song

et al. 2005

Bioprocess Biosyst Eng

View full text Add to dashboard Cite

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“…[4][5][6][7] Moreover, it may be employed in many other reactions, like the synthesis of antibiotics, resolution of racemic mixtures, synthesis of amides and selective deprotections. [8][9][10][11][12][13][14][15] Although PGA has a moderate thermostability which has permitted its rapid implementation in hydrolytic reactions, it is rapidly inactivated by most of the currently used organic cosolvents or in anhydrous media, [16][17][18][19][20] reaction conditions which are required for antibiotic synthesis to shift thermodynamic equilibrium in the synthetic direction or to increase the solubility of hydrophobic compounds. [14,[21][22][23][24][25][26] One strategy to improve the enzyme stability in organic media may be to generate hydrophilic environments around the enzyme, promoting a certain partition of the organic solvent molecules and a drop in the organic solvent concentration in the enzyme environment.…”

Section: Introductionmentioning

confidence: 99%

Improved Stabilization of Genetically Modified Penicillin G Acylase in the Presence of Organic Cosolvents by Co‐ Immobilization of the Enzyme with Polyethyleneimine

et al. 2007

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Penicillin G acylase (PGA) is an enzyme that hardly interacts with polycationic polymers (e.g., polyethyleneimine, PEI) and thus the enzyme cannot be stabilized against the action of organic solvents by its co-immobilization with the polymer in the same support, neither covalently attached to the support nor adsorbed on the already immobilized enzyme. However, a new mutant PGA bearing eight additional Glu residues homogenously distributed throughout the enzyme surface may interact with the polymer. The co-immobilization of the enzyme and PEI on glyoxyl-agarose allows one to fully take advantage of the stabilization produced by the multipoint covalent attachment and by the protective hydrophilic micro-environment generated by the polycationic polymer, enabling a significant stabilization of the immobilized PGA in the presence of organic solvents.

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“…Moreover, it is a useful biocatalyst in peptide synthesis (Khimiuk et al 2003) and resolution of racemic compounds (Van Langen et al 2000). Penicillin G acylase (PGA) has been found in various bacteria and fungi.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of permeabilized whole cell penicillin G acylase from Alcaligenes faecalis using pore matrix crosslinked with glutaraldehyde

et al. 2006

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The activity of penicillin G acylase from Alcaligenes faecalis increased 7.5-fold when cells were permeabilized with 0.3% (w/v) CTAB. The treated cells were entrapped by polyvinyl alcohol crosslinked with boric acid, and crosslinked with 2% (v/v) glutaraldehyde to increase the stability. The conversion yield of penicillin G to 6-aminopenicillanic acid was 75% by immobilized system in batch reaction. No activity was lost after 15 cycles and about 65% enzyme activity was retained at the end of the 31th cycle.

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Penicillin acylase-catalyzed resolution of amines in aqueous organic solvents

Cited by 62 publications

References 29 publications

Effect of organic cosolvent on kinetic resolution of tert-leucine by penicillin G acylase from Kluyvera citrophila

Effect of organic cosolvent on kinetic resolution of tert-leucine by penicillin G acylase from Kluyvera citrophila

Improved Stabilization of Genetically Modified Penicillin G Acylase in the Presence of Organic Cosolvents by Co‐ Immobilization of the Enzyme with Polyethyleneimine

Immobilization of permeabilized whole cell penicillin G acylase from Alcaligenes faecalis using pore matrix crosslinked with glutaraldehyde

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