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Applied and Environmental Microbiology, January 2009, p. 514-520, Vol. 75, No. 2
0099-2240/09/$08.00+0     doi:10.1128/AEM.01128-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Potential Application of N-Carbamoyl-β-Alanine Amidohydrolase from Agrobacterium tumefaciens C58 for β-Amino Acid Production{triangledown}

Ana Isabel Martínez-Gómez,1 Sergio Martínez-Rodríguez,1 Joaquín Pozo-Dengra,1 Davide Tessaro,2 Stefano Servi,2 Josefa María Clemente-Jiménez,1 Felipe Rodríguez-Vico,1 and Francisco Javier Las Heras-Vázquez1*

Departamento de Química-Física, Bioquímica y Química Inorgánica, Edificio CITE I, Universidad de Almería, La Cañada de San Urbano, E-04120 Almería, Spain,1 Dipartimento di Chimica, Materiali, Ingegneria Chimica G. Natta, Politecnico di Milano, Milan, Italy2

Received 19 May 2008/ Accepted 10 November 2008

An N-carbamoyl-β-alanine amidohydrolase of industrial interest from Agrobacterium tumefaciens C58 (βcarAt) has been characterized. βcarAt is most active at 30°C and pH 8.0 with N-carbamoyl-β-alanine as a substrate. The purified enzyme is completely inactivated by the metal-chelating agent 8-hydroxyquinoline-5-sulfonic acid (HQSA), and activity is restored by the addition of divalent metal ions, such as Mn2+, Ni2+, and Co2+. The native enzyme is a homodimer with a molecular mass of 90 kDa from pH 5.5 to 9.0. The enzyme has a broad substrate spectrum and hydrolyzes nonsubstituted N-carbamoyl-{alpha}-, -β-, -{gamma}-, and -{delta}-amino acids, with the greatest catalytic efficiency for N-carbamoyl-β-alanine. βcarAt also recognizes substrate analogues substituted with sulfonic and phosphonic acid groups to produce the β-amino acids taurine and ciliatine, respectively. βcarAt is able to produce monosubstituted β2- and β3-amino acids, showing better catalytic efficiency (kcat/Km) for the production of the former. For both types of monosubstituted substrates, the enzyme hydrolyzes N-carbamoyl-β-amino acids with a short aliphatic side chain better than those with aromatic rings. These properties make βcarAt an outstanding candidate for application in the biotechnology industry.

* Corresponding author. Mailing address: Departamento de Química-Física, Bioquímica y Química Inorgánica, Edificio CITE I, Universidad de Almería, La Cañada de San Urbano, E-04120 Almería, Spain. Phone: 34 950 015055. Fax: 34 950 015008. E-mail: fjheras{at}ual.es

{triangledown} Published ahead of print on 14 November 2008.

Applied and Environmental Microbiology, January 2009, p. 514-520, Vol. 75, No. 2
0099-2240/09/$08.00+0     doi:10.1128/AEM.01128-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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