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Alloyed Trimetallic Nanocomposite as an Efficient and Recyclable Solid Matrix for Ideonella sakaiensis Lipase Immobilization.
Addai, Frank Peprah; Wu, Jiacong; Lin, Feng; Ma, Xinnan; Han, Juan; Liu, Yuelin; Zhou, Yang; Wang, Yun.
Afiliación
  • Addai FP; School of Chemistry and Chemical Engineering, Jiangsu University, Zhenjiang, Jiangsu 212013, China.
  • Wu J; School of Life Sciences, Jiangsu University, Zhenjiang, Jiangsu 212013, China.
  • Lin F; School of Chemistry and Chemical Engineering, Jiangsu University, Zhenjiang, Jiangsu 212013, China.
  • Ma X; Key Laboratory of Healthy Freshwater Aquaculture, Ministry of Agriculture, Zhejiang Institute of Freshwater Fisheries, Zhejiang, Huzhou 313001, China.
  • Han J; School of Chemistry and Chemical Engineering, Jiangsu University, Zhenjiang, Jiangsu 212013, China.
  • Liu Y; School of Food and Biological Engineering, Jiangsu University, Zhenjiang, Jiangsu 212013, China.
  • Zhou Y; School of Life Sciences, Jiangsu University, Zhenjiang, Jiangsu 212013, China.
  • Wang Y; School of Life Sciences, Jiangsu University, Zhenjiang, Jiangsu 212013, China.
Langmuir ; 40(17): 8921-8938, 2024 Apr 30.
Article en En | MEDLINE | ID: mdl-38626327
ABSTRACT
In this work, a trimetallic (Ni/Co/Zn) organic framework (tMOF), synthesized by a solvothermal method, was calcinated at 400 and 600 °C and the final products were used as a support for lipase immobilization. The material annealed at 400 °C (Ni-Co-Zn@400) had an improved surface area (66.01 m2/g) and pore volume (0.194 cm3/g), which showed the highest enzyme loading capacity (301 mg/g) with a specific activity of 0.196 U/mg, and could protect the enzyme against thermal denaturation at 65 °C. The optimal pH and temperature for the lipase were 8.0 and 45 °C but could tolerate pH levels 7.0-8.0 and temperatures 40-60 °C. Moreover, the immobilized enzyme (Ni-Co-Zn@Lipase, Ni-Co-Zn@400@Lipase, or Ni-Co-Zn@600@Lipase) could be recovered and reused for over seven cycles maintaining 80, 90, and 11% of its original activity and maintained a residual activity >90% after 40 storage days. The remarkable thermostability and storage stability of the immobilized lipase suggest that the rigid structure of the support acted as a protective shield against denaturation, while the improved pH tolerance toward the alkaline range indicates a shift in the ionization state attributed to unequal partitioning of hydroxyl and hydrogen ions within the microenvironment of the active site, suggesting that acidic residues may have been involved in forming an enzyme-support bond. The high enzyme loading capacity, specific activity, encouraging stability, and high recoverability of the tMOF@Lipase indicate that a multimetallic MOF could be a better platform for efficient enzyme immobilization.
Asunto(s)

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Zinc / Enzimas Inmovilizadas / Nanocompuestos / Lipasa Idioma: En Revista: Langmuir Asunto de la revista: QUIMICA Año: 2024 Tipo del documento: Article País de afiliación: China

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Zinc / Enzimas Inmovilizadas / Nanocompuestos / Lipasa Idioma: En Revista: Langmuir Asunto de la revista: QUIMICA Año: 2024 Tipo del documento: Article País de afiliación: China