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Development of chia gum/alginate-polymer support for horseradish peroxidase immobilization and its application in phenolic removal.
Mohamed, Saleh A; Elsayed, Alshaimaa M; Salah, Hala A; Barakat, Amal Z; Bassuiny, Roqaya I; Abdel-Mageed, Heidi M; Abdel-Aty, Azza M.
Afiliación
  • Mohamed SA; Molecular Biology Department, National Research Centre, Dokki, Cairo, Egypt. saleh38@hotmail.com.
  • Elsayed AM; Molecular Biology Department, National Research Centre, Dokki, Cairo, Egypt.
  • Salah HA; Molecular Biology Department, National Research Centre, Dokki, Cairo, Egypt.
  • Barakat AZ; Molecular Biology Department, National Research Centre, Dokki, Cairo, Egypt.
  • Bassuiny RI; Molecular Biology Department, National Research Centre, Dokki, Cairo, Egypt.
  • Abdel-Mageed HM; Molecular Biology Department, National Research Centre, Dokki, Cairo, Egypt.
  • Abdel-Aty AM; Molecular Biology Department, National Research Centre, Dokki, Cairo, Egypt.
Sci Rep ; 14(1): 1362, 2024 01 16.
Article en En | MEDLINE | ID: mdl-38228654
ABSTRACT
Chia gum's molecular structure with distinctive properties as well as the alginate-based hydrogel's three-dimensionally cross-linked structure can provide a potent matrix for immobilization of enzyme. Herein, chia gum (CG)/alginate (A)-polymeric complex was synthesized and employed as a support material for the immobilization of horseradish peroxidase (HRP). HRP was successfully immobilized on the developed ACG-polymeric support, and the highest immobilization recovery (75%) was observed at 1.0% CG and 2% A, pH 7.0, and 50 units of the enzyme. The structure, morphology, and thermal properties of the prepared ACG-HRP were demonstrated using Fourier Transform Infrared (FTIR), Scanning Electron Microscope, and Thermogravimetric (TGA) analyses. ACG-HRP showed a good reusability (60%) over ten reuses. The immobilized ACG-HRP displayed an acidic pH optimum (6.0), a higher temperature optimum (50 °C), and improved thermal stability (30-50 °C) compared to the soluble HRP at pH 7.0, 40 °C and (30-40 °C), respectively. ACG-HRP has a lower affinity for hydrogen peroxide (H2O2) and guaiacol and a higher oxidizing affinity for a number of phenolic substrates. The ACG-HRP demonstrated greater resistance to heavy metals, isopropanol, urea, Triton X-100, and urea, as well as improved efficiency for eliminating phenol and p-chlorophenol. The developed ACG-polymeric support provided improved enzyme properties, allowed the reuse of the immobilized HRP in 10 cycles, and made it promising for several biotechnological applications.
Asunto(s)

Texto completo: 1 Base de datos: MEDLINE Asunto principal: Polímeros / Enzimas Inmovilizadas Idioma: En Revista: Sci Rep Año: 2024 Tipo del documento: Article

Texto completo: 1 Base de datos: MEDLINE Asunto principal: Polímeros / Enzimas Inmovilizadas Idioma: En Revista: Sci Rep Año: 2024 Tipo del documento: Article