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Título: | Glyoxyl-Activated Agarose as Support for Covalently Link Novo-Pro D: Biocatalysts Performance in the Hydrolysis of Casein |
Autor: | Antunes Lopes, Laiane; Kern Novelli, Paula; Fernández-Lafuente, Roberto CSIC ORCID; Waldir Tardioli, Paulo; Camargo Giordano, Raquel Lima | Palabras clave: | Enzyme immobilization Enzyme stabilization Protease Protein hydrolysis Agarose-glyoxyl |
Fecha de publicación: | 2020 | Editor: | Multidisciplinary Digital Publishing Institute | Citación: | Catalysts 10(5): 466 (2020) | Resumen: | This study aimed to evaluate the performance of a commercial protease (Novo-Pro D (NPD)), both in soluble and immobilized forms, in the hydrolysis of proteins (using casein as model protein). Immobilization of the protease NPD on 6% agarose activated with glyoxyl groups for 24 h at 20 °C and pH 10.0 allowed preparing immobilized biocatalyst with around 90% immobilization yield, 92% recovered activity versus small substrate, and a thermal stability 5.3-fold higher than the dialyzed soluble enzyme at 50 °C and pH 8.0. Immobilization times longer than 24 h lead to a decrease in the recovered activity and did not improve the biocatalyst stability. At 50 °C and pH 6.5, the immobilized NPD was around 20-fold more stable than the dialyzed soluble protease. Versus casein, the immobilized NDP presented a 10% level of activity, but it allowed hydrolyzing casein (26 g/L) at 50 °C and pH 6.5 up to a 40% degree of hydrolysis (DH) after 2 h reaction, while under the same conditions, only a 34% DH was achieved with soluble NPD. In addition, the immobilized NPD showed good reusability, maintaining the DH of casein for at least ten 2h-reaction batches. | Descripción: | © 2020 by the authors. | Versión del editor: | https://doi.org/10.3390/catal10050466 | URI: | http://hdl.handle.net/10261/212505 | DOI: | 10.3390/catal10050466 | ISSN: | 2073-4344 | E-ISSN: | 2073-4344 |
Aparece en las colecciones: | (ICP) Artículos |
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Glyoxyl-Activated_Antunes_Art2020.pdf | 3,57 MB | Adobe PDF | Visualizar/Abrir |
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