Biochemical Evaluation of Phenylalanine Ammonia Lyase from Endemic Plant (Bunge) Aellen. for the Dietary Treatment of Phenylketonuria.

Enzyme substitution therapy with the phenylalanine ammonia lyase (PAL) is a new approach to the treatment of patients with phenylketonuria (PKU). This enzyme is responsible for the conversion of phenylalanine to -cinnamic acid. We assessed the PAL enzyme of the endemic plant (Bunge) Aellen.

Biochemical analysis of Centaurea depressa phenylalanine ammonia lyase (PAL) for biotechnological applications in phenylketonuria (PKU).

Context: Phenylketonuria (PKU) is the most common hereditary defect of phenylalanine hydroxylase (PAH) enzyme achieving the hydroxylation of phenylalanine (Phe). Phenylalanine ammonia lyase (PAL) converts Phe to a harmless metabolite, trans-cinnamic acid (TCA) in plants and PAL enzyme activity is fairly high in plants rich in flavonoids.

Objective: The study aimed the biochemical analysis of PAL form Centaurea depressa BIEB.

Mechanisms of cholesterol-lowering effects of lactobacilli and bifidobacteria strains as potential probiotics with their bsh gene analysis.

The bile salt hydrolase (BSH) enzyme activities of human-derived lactic acid bacteria and bifidobacteria were evaluated. The highest enzyme activity was identified as 1.76 ± 0.

Phenylalanine ammonia lyase (PAL) enzyme activity and antioxidant properties of some cyanobacteria isolates.

In the present study, six cyanobacteria isolates were evaluated for the PAL enzyme activity, and their methanol extracts were assessed for the total phenolic amount and other antioxidant parameters. Synechocystis sp. BASO444 and Synechocystis sp.