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Glyoxyl-Activated Agarose as Support for Covalently Link Novo-Pro D: Biocatalysts Performance in the Hydrolysis of Casein

AuthorsAntunes Lopes, Laiane; Kern Novelli, Paula; Fernández-Lafuente, Roberto ; Waldir Tardioli, Paulo; Camargo Giordano, Raquel Lima
KeywordsEnzyme immobilization
Enzyme stabilization
Protein hydrolysis
Issue Date2020
PublisherMultidisciplinary Digital Publishing Institute
CitationCatalysts 10(5): 466 (2020)
AbstractThis 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.
Description© 2020 by the authors.
Publisher version (URL)https://doi.org/10.3390/catal10050466
Appears in Collections:(ICP) Artículos
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