Article Abstract:
The degradation of ferulic acid in the Pseudomonas putida is under the control of several genes in the bacterial genome. The genes were identified in a Tn5 genomic mutant bank. Four genes were identified to be determinants in the bioconversion of ferulic acid to protocatechuic acid. These are fca, vdh, vanA and vanB. The first two genes codes for proteins responsible for the synthesis of vanillic acid from ferulic acid while the last two genes codes for proteins that demethylate vanillic acid to yield protocatechuic acid.
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Article Abstract:
Standard techniques help purify an enzyme from Bacillus pumilus PS213, which is responsible for the nonoxidative decarboxylation of ferulic acid and p-coumaric acid producing 4-vinylguaiacol and 4-vinylphenol, respectively. Purified enzyme exhibits a single band of 23 kDa and size exclusion chromatography reveals the molecular mass of the enzyme as 45 kDa. Addition of cation exerts no influence on the enzyme activity, which is maximum at 37 degrees Celsius and pH 5.5.
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Article Abstract:
A Bacillus pumilus 3,690-bp HindIII fragment containing the gene encoding ferulic acid decarboxylase (fdc) stimulates ferulic acid decarboxylation when expressed in Escherichia coli. The DNA fragment contains a Shine-Dalgarno sequence and a promoter sequence. The fdc has an apparent molecular mass of 42 kDa and is a homodimer. The B. pumilus fdc is structurally similar to the E. coli enzyme and 66.7% identical to yeast phenylacrylic decarboxylases.
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