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Author: search.filters.author.Leksawasdi, NoppolSubject: search.filters.subject.Pyruvate decarboxylase

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    Development of mathematical model for pyruvate decarboxylase deactivation kinetics by benzaldehyde with inorganic phosphate activation effect
    (2018-05-01)
    Khemacheewakul, Julaluk
    ;
    Techapun, Charin
    ;
    Kuntiya, Ampin
    ;
    Sanguanchaipaiwong, Vorapat
    ;
    Chaiyaso, Thanongsak
    The effect of phosphate concentrations at 20, 250, 500, and 1,000 mM on phenylacetylcarbinol (PAC) production, pyruvate decarboxylase (PDC) deactivation kinetics, and combination of phosphate activation effect in a mathematical model were evaluated in a biotransformation system using whole cells of Candida tropicalis TISTR 5350. This is the first report of phosphate activation effect on pyruvate decarboxylase deactivation model. The highest PAC concentration (28.6 ± 2.3 mM), average instantaneous PAC formation rate (0.57 ± 0.01 mM/min), PAC yields (0.95 ± 0.08 on benzaldehyde and 0.71 ± 0.06 on pyruvate) were achieved in 1,000 mM phosphate buffer. PDC volumetric activity of 0.52 ± 0.07 U carboligase/ml at the reaction time of 180 min was obtained. The mathematical model describing deactivation kinetics of whole cells PDC by benzaldehyde with activation effect for phosphate buffer concentration level predicted individual experimental data for all four levels of phosphate buffer relatively well with corresponding residual sum of square (RSS), mean square (MS), and correlation coefficient (R<sup>2</sup>) range of 213-1,100, 5.32-27.5, and 0.96-0.99. The activation effect of 1,000 mM phosphate buffer was evident with an average enzyme activation rate constant due to buffering species concentration level (K<inf>a</inf>) of 1.34 × 10<sup>-2</sup> % min<sup>-1</sup> which was higher than 20 mM phosphate buffer (1.48 × 10<sup>-6</sup> % min<sup>-1</sup>) by more than 9,050 times.
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    Partial purification and comparison of precipitation techniques of pyruvate decarboxylase enzyme
    (2017-01-01)
    Tangtua, Julaluk
    ;
    Techapun, Charin
    ;
    Pratanaphon, Ronachai
    ;
    Kuntiya, Ampin
    ;
    Sanguanchaipaiwong, Vorapat
    The intracellular pyruvate decarboxylase enzyme (PDC, EC 4.1.1.1) extract from Candida tropicalis TISTR 5350 was compared by two different purification methods using ammonium sulphate and acetone precipitation. The total volumetric PDC activity and percentage recovery (yield) of precipitated PDC based on 50% (v/v) cold acetone were significantly higher (1.13 ± 0.02 U/ml and 98.27 ± 2.98 %, respectively) than any other concentration levels of acetone used. Furthermore, all concentration levels of cold acetone also yielded a much higher specific PDC activity than the precipitate obtained using the 40 to 60% (w/v) ammonium sulphate saturation (0.75 ± 0.08 U/mg protein). The precipitated enzyme in buffer solutions from the 50% (v/v) acetone was subsequently freeze dried. Freeze drying of the precipitated PDC by cold acetone resulted in the specific PDC activity of 1.57 ± 0.02 U/mg protein and differed statistically (p ≤ 0.05) from the crude enzyme extract (control).
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    Evaluation of cell disruption for partial isolation of intracellular pyruvate decarboxylase enzyme by silver nanoparticles method
    (2015-07-01)
    Tangtua, J.
    ;
    Techapun, C.
    ;
    Pratanaphon, R.
    ;
    Kuntiya, A.
    ;
    Chaiyaso, T.
    Candida tropicalis TISTR 5350 was used in the comparison of seven concentration levels of silver nanoparticles (0, 5, 10, 15, 20, 25, and 30 μg ml-1) for cell disruption methods. The optimized cell disruption strategy was selected based on the optimal protein yield and biological activity. The maximum volumetric and specifi c pyruvate decarboxylase (PDC, EC 4.1.1.1) activities (0.53±0.05 U ml-1 and 0.17±0.02 U mg-1 protein, respectively) were observed at 15 μg ml-1 silver nanoparticles. The silver nanoparticle concentration level of 15 μg ml-1 was investigated further by comparing the reaction mixtures at different time intervals of 0, 1, 2, 3, 4, 5, and 6 min. The result showed that the highest specifi c PDC activity of 0.39±0.01 U mg-1 protein was obtained from mixing for 3 min. This was not significantly different (P≤0.05) from other mixing time intervals.