Enhancing the activity of biocatalysts supported on calcium phosphate by inducing mesoporosity with phosphopeptides

• Published in: Colloids and surfaces. A, Physicochemical and engineering aspects Physicochemical and engineering aspects, 2023-03, Vol.660, p.130906, Article 130906
• Main Authors: Dhayal, Surender Kumar, Lund, Martin, van den Brink, J.M., Medjahdi, Ghouti, Celzard, Alain, Fierro, Vanessa, Gardiennet, Carole, Pasc, Andreea, Canilho, Nadia
• Format: Article
• Language: English
• Subjects: Biomaterial; Biomineralization; Chemical Sciences; Enzymatic supported catalyst; Hydroxyapatite-like nanoparticles
• ISSN: 0927-7757; 1873-4359
• DOI: 10.1016/j.colsurfa.2022.130906

Preventing enzyme deactivation while increasing their accessibility by adsorption in mesopores remains a key challenge in the design of biocompatible supported enzymatic catalysts. Herein, it is expected that food-grade monomeric or polymeric glycopeptides containing organic phosphate groups (as casein phosphopeptide derivatives) enhances the entrapment of the enzyme over the one pot method of wet precipitation of calcium phosphate (CaP) leading to a biocompatible hybrid organic/inorganic catalyst. The supported catalyst was prepared by wet precipitation of calcium and phosphorous in the presence of either monomeric glycopeptide or polymeric glycopeptide. These organic glycopeptides had an influence on the electrostatic stabilization during the nucleation of calcium phosphate particles, as tracked by dynamic light scattering and by scanning electron microscopy.The phosphopeptide derivatives, were able to decrease the crystallization degree in calcium phosphate particles, as demonstrated by XRD and solid-state NMR analysis. Furthermore, according to N2 sorption data, the glycopeptide derivatives induced interparticle mesopores, which might be responsible of the enhanced enzymatic activity of the supported biocatalyst that improved from 52 (+/−19) NLU·g−1 without organic compound to 607 (+/−34) NLU·g−1. [Display omitted]