Structural Characterization of β-Xylosidase XynB2 from Geobacillus stearothermophilus CECT43: A Member of the Glycoside Hydrolase Family GH52

Autor: Jose Antonio Gavira, Lellys M. Contreras, Hassan Mohamad Alshamaa, Josefa María Clemente-Jiménez, Felipe Rodríguez-Vico, Francisco Javier Las Heras-Vázquez, Sergio Martínez-Rodríguez

Publikováno v: Crystals, Vol 14, Iss 1, p 18 (2023)

β-xylosidases (4-β-d-xylan xylohydrolase, E.C. 3.2.1.37) are glycoside hydrolases (GH) catalyzing the hydrolysis of (1→4)-β-d-xylans, allowing for the removal of β-d-xylose residues from its non-reducing termini. Together with other xylan-degra

Externí odkaz: https://doaj.org/article/6401a6af132842068c72e731a1f28493

Immobilized Double-Racemase Hydantoinase Process for L-Amino Acid Production

Autor: Francisco Javier Las Heras-Vázquez, Lellys Mariela Contreras Moyeja, Josefa María Clemente-Jiménez, Felipe Rodríguez-Vico

Protein immobilization is proving to be an environmentally friendly strategy for manufacturing biochemicals at high yields and low production costs. This work describes the optimization of the so-called “double-racemase hydantoinase process,” a s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcd13f573ba1a01815e942a354db4c2a

Rational re-design of the 'double-racemase hydantoinase process' for optically pure production of natural and non-natural l-amino acids

Autor: María José Rodríguez-Alonso, Josefa María Clemente-Jiménez, Felipe Rodríguez-Vico, Francisco Javier Las Heras Vázquez

Publikováno v: Biochemical Engineering Journal. 101:68-76

The “hydantoinase process” is a well-established method for the industrial production of optically pure d -amino acids. However, due to the strict d -enantioselectivity of most hydantoinase enzymes, the process is less efficient for l -amino acid

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::113c3bc8fdb201dcd4114d196560d0c9
https://doi.org/10.1016/j.bej.2015.05.003

l-Amino Acid Production by a Immobilized Double-Racemase Hydantoinase Process: Improvement and Comparison with a Free Protein System

Autor: Francisco Javier Las Heras-Vázquez, María José Rodríguez-Alonso, Josefa María Clemente-Jiménez, Felipe Rodríguez-Vico

Publikováno v: Catalysts 7(6), 192 (2017)
Helvia. Repositorio Institucional de la Universidad de Córdoba
instname
Catalysts; Volume 7; Issue 6; Pages: 192
Helvia: Repositorio Institucional de la Universidad de Córdoba
Universidad de Córdoba
riUAL. Repositorio Institucional de la Universidad de Almería
Universidad de Almería
Catalysts, Vol 7, Iss 6, p 192 (2017)

Protein immobilization is proving to be an environmentally friendly strategy for manufacturing biochemicals at high yields and low production costs. This work describes the optimization of the so-called “double-racemase hydantoinase process,” a s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31b1757d74bfa8c825dc99ffc7d0b0f0
http://hdl.handle.net/10835/7416

Biochemical and mutational studies of allantoinase from Bacillus licheniformis CECT 20T

Autor: Ana Isabel Martínez-Gómez, Francisco Javier Las Heras-Vázquez, Montserrat Andújar-Sánchez, José L. Neira, Sergio Martínez-Rodríguez, Josefa María Clemente-Jiménez, Felipe Rodríguez-Vico, Pablo Soriano-Maldonado

Publikováno v: Biochimie. 99:178-188

Allantoinases (allantoin amidohydrolase, E.C. 3.5.2.5) catalyze the hydrolysis of the amide bond of allantoin to form allantoic acid, in those organisms where allantoin is not the final product of uric acid degradation. Despite their importance in th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b390581f8188098acd547e96ddb6c46d
https://doi.org/10.1016/j.biochi.2013.12.002