Metabolism of DL-(+/-)-phenylalanine by Aspergillus niger.

AUTOR(ES)

Kishore, G

RESUMO

A fungus capable of degrading DL-phenylalanine was isolated from the soil and identified as Aspergillus niger. It was found to metabolize DL-phenylalanine by a new pathway involving 4-hydroxymandelic acid. D-Amino acid oxidase and L-phenylalanine: 2-oxoglutaric acid aminotransferase initiated the degradation of D- and L-phenylalanine, respectively. Both phenylpyruvate oxidase and phenylpyruvate decarboxylase activities could be demonstrated in the cell-free system. Phenylacetate hydroxylase, which required reduced nicotinamide adenine dinucleotide phosphate, converted phenylacetic acid to 2- and 4-hydroxyphenylacetic acid. Although 4-hydroxyphenylacetate was converted to 4-hydroxymandelate, 2-hydroxyphenylacetate was not utilized until the onset of sporulation. During sporulation, it was converted rapidly into homogentisate and oxidized to ring-cleaved products. 4-Hydroxymandelate was degraded to protocatechuate via 4-hydroxybenzoylformate, 4-hydroxybenzaldehyde, and 4-hydroxybenzoate.

Documentos Relacionados

• Ochratoxin A production by strains of Aspergillus niger var. niger.
• Chronic necrotising pneumonia caused by Aspergillus niger.
• Aconitase and citric acid fermentation by Aspergillus niger.
• Degradation of the plant flavonoid phellamurin by Aspergillus niger.
• Studies on the biosynthesis of aspergillin by Aspergillus niger.