Publicaciones en colaboración con investigadores/as de Cornell University (11)

2007

  1. Phytase: Source, structure and application

    Industrial Enzymes: Structure, Function and Applications (Springer Netherlands), pp. 505-529

2006

  1. Shifting the pH profile of Aspergillus niger PhyA phytase to match the stomach pH enhances its effectiveness as an animal feed additive

    Applied and Environmental Microbiology, Vol. 72, Núm. 6, pp. 4397-4403

2003

  1. Phytase enzymology, applications, and biotechnology

    Biotechnology Letters, Vol. 25, Núm. 21, pp. 1787-1794

2002

  1. Functional expression of keratinase (kerA) gene from Bacillus licheniformis in Pichia pastoris

    Biotechnology Letters, Vol. 24, Núm. 8, pp. 631-636

  2. Site-directed mutagenesis of Aspergillus niger NRRL 3135 phytase at residue 300 to enhance catalysis at pH 4.0

    Biochemical and Biophysical Research Communications, Vol. 297, Núm. 4, pp. 1016-1020

2001

  1. Comparative impacts of glutathione peroxidase-1 gene knockout on oxidative stress induced by reactive oxygen and nitrogen species in mouse hepatocytes

    Biochemical Journal, Vol. 359, Núm. 3, pp. 687-695

  2. Phytase and citric acid supplementation in whole-wheat bread improves phytatephosphorus release and iron dialyzability

    Journal of Food Science, Vol. 66, Núm. 4, pp. 614-619

1999

  1. Dietary intrinsic phytate protects colon from lipid peroxidation in pigs with a moderately high dietary iron intake

    Proceedings of the Society for Experimental Biology and Medicine, Vol. 221, Núm. 1, pp. 80-86

  2. Different sensitivity of recombinant Aspergillus niger phytase (r-PhyA) and Escherichia coli pH 2.5 acid phosphatase (r-AppA) to trypsin and pepsin in vitro

    Archives of Biochemistry and Biophysics, Vol. 365, Núm. 2, pp. 262-267

  3. Knockout of cellular glutathione peroxidase gene renders mice susceptible to diquat-induced oxidative stress

    Free Radical Biology and Medicine, Vol. 27, Núm. 5-6, pp. 605-611

  4. Selenium-dependent cellular glutathione peroxidase protects mice against a pro-oxidant-induced oxidation of NADPH, NADH, lipids, and protein

    FASEB Journal, Vol. 13, Núm. 11, pp. 1467-1475