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[Catalytic properties of Rhodotorula aurantiaca KM-1 phenylalanine ammonia-lyase]

I L Bazukian, A E Vardanian, A A Ambartsumian

    Prikladnaia Biokhimiia I Mikrobiologiia
    |February 25, 2009
    PubMed

    Insights

    Rhodotorula aurantiaca strain KM-1

    Area of Science:

    • Biochemistry
    • Enzymology

    Context:

    • Characterizing L-phenylalanine ammonia-lyase (PAL) from Rhodotorula aurantiaca KM-1.
    • Investigating enzyme kinetics and stability under various conditions.

    Purpose:

    • To determine the kinetic parameters (K(M), V(max)) of PAL.
    • To identify PAL's inhibition type and calculate inhibition constants.
    • To assess PAL's stability and factors influencing L-phenylalanine yield.

    Summary:

    • L-phenylalanine ammonia-lyase (PAL) from Rhodotorula aurantiaca KM-1 follows Michaelis-Menten kinetics.
    • The enzyme is competitively inhibited by D-phenylalanine.
    • PAL exhibits optimal stability at pH 6.55 and is stabilized by mercaptoethanol, EDTA, and ascorbic acid, enhancing L-phenylalanine yield.

    Impact:

    • Provides detailed kinetic and stability data for Rhodotorula aurantiaca PAL.
    • Identifies key factors for optimizing L-phenylalanine production using this enzyme.
    • Contributes to understanding enzyme mechanisms and applications in biocatalysis.

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