NDLI: Gene cloning, expression, and characterization of phenolic acid decarboxylase from Lactobacillus brevis RM84

Content Provider	Springer Nature Link
Author	Landete, José María Rodríguez, Héctor Curiel, José Antonio Rivas, Blanca Mancheño, José Miguel Muñoz, Rosario
Copyright Year	2010
Abstract	Phenolic acid decarboxylase (PAD) catalyzes the synthesis of vinyl phenols from hydroxycinnamic acids. The gene encoding PAD from Lactobacillus brevis was cloned and expressed as a fusion protein in Escherichia coli. The recombinant PAD enzyme is a heat-labile enzyme that functions optimally at 22°C and pH 6.0. The purified enzyme did not show thermostability at temperatures above 22°C. L. brevis PAD is able to decarboxylate exclusively the hydroxycinnamic acids, such as p-coumaric, caffeic, and ferulic acids, with K m values of 0.98, 0.96, and 0.78 mM, respectively. The substrate specificity exhibited by L. brevis PAD is similar to the PAD isolated from Bacillus subtilis and B. pumilus, but different from that of L. plantarum and Pediococcus pentosaceus. As the C-terminal region may be involved in determining PAD substrate specificity and catalytic capacity, amino acid differences among these proteins could explain the differences observed. The substrate specificity shown by L. brevis PAD shows promise for the synthesis of high-added value products from plant wastes.
Starting Page	617
Ending Page	624
Page Count	8
File Format	PDF
ISSN	13675435
Journal	Journal of Industrial Microbiology and Biotechnology
Volume Number	37
Issue Number	6
e-ISSN	14765535
Language	English
Publisher	Springer-Verlag
Publisher Date	2010-03-24
Publisher Place	Berlin, Heidelberg
Access Restriction	Subscribed
Subject Keyword	p-Coumaric acid Ferulic acid Phenolic acid decarboxylase Phenolic acids Vinyl phenol Microbiology Bioinformatics Biotechnology Genetic Engineering Inorganic Chemistry Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Bioengineering Applied Microbiology and Biotechnology Biotechnology

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