Kinetics of deactivation of l-lysinamidase, l-aminoacylase and d-hydantoinase

Dagys, Rimantas; Žvirblis, S.; Lukša, Virginijus; Pauliukonis, A.

doi:10.1016/0168-1656(92)90073-i

Cited by 3 publications

(1 citation statement)

References 15 publications

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“…This method is included in the program EnzFitter from Biosoft,13 which provides confidence limits for a confidence level of 95%. Moreover, the direct linear plot proposed by Cornish‐Bowden,14 included in the program EnzPack from Biosoft,15 has been used. This program establishes the confidence levels as a function of the obtained results.…”

Section: Resultsmentioning

confidence: 99%

Kinetics of the L‐aminoacylase‐catalyzed resolution of N‐acetyl‐DL‐butyrine

Bódalo

Gómez

Máximo

et al. 2002

J of Chemical Tech & Biotech

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The kinetics of the asymmetric hydrolysis of N-acetyl-DL-butyrine catalyzed by L-amino-acylase to obtain optically pure L-butyrine is described. Some of the constants are determined from the initial reaction rates and others from long-term experiments in batch reactors by the numerical integration of the reactor design equation and minimization of the kinetic parameters. The methodology described can be applied to the kinetic study of other complex biocatalytic systems. Studies on enzyme activation by adding different divalent metal ions and enzymatic deactivation are also included. # 2002 Society of Chemical Industry Keywords: kinetics; DL-butyrine; resolution; L-aminoacylase; enzyme deactivationInitial rate referring to the quantity of enzyme (mmol minInitial rate referred to the quantity of enzyme at t = 0, in absence of deactivationMaximum enzymatic rate at t = 0, in absence of deactivation (mmol dmMaximum rate referred to the quantity of enzyme at t = 0, in absence of deactivation (mmol min À1 mgE À1

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Section: Resultsmentioning

confidence: 99%

Kinetics of the L‐aminoacylase‐catalyzed resolution of N‐acetyl‐DL‐butyrine

Bódalo

Gómez

Máximo

et al. 2002

J of Chemical Tech & Biotech

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Purification and characterization of theD-hydantoinase from bacillus circulans

Lukša¹,

Starkuviene²,

StarkuvienE³

et al. 1997

Appl Biochem Biotechnol

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A D-hydantoinase (5,6-dihydropyrimidine amidohydrolase) was purified to homogeneity from Bacillus circulans. Purification of two hundred forty-three-fold was achieved with an overall yield of 12%. The relative molecular mass of the native enzyme is 212,000 and that of the subunit is 53,000. This enzyme is an acidic protein with an isoelectric point of 4.55. The enzyme is sensitive to thiol reagent and requires metal ions for its activity. The optimal conditions for the hydantoinase activity are pH 8.0-10.0 and a temperature of 75 degrees C. The enzyme is the most stable in a pH range of 8.5-9.5 and up to 60 degrees C. The enzyme is significantly stable not only at high temperatures but also on treatment with protein denaturant SDS. These remarkable properties are used for the purification procedure.

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