Preparation and characterization of stable core/shell FeO@Au decorated with an amine group for immobilization of lipase by covalent attachment

• Published in: RSC advances Vol. 12; no. 1; pp. 5971 - 5977
• Main Authors: Aghamolaei, Marziyeh, Landarani-Isfahani, Amir, Bahadori, Mehrnaz, Nori, Zahra Zamani, Rezaei, Saghar, Moghadam, Majid, Tangestaninejad, Shahram, Mirkhani, Valiollah, Mohammadpoor-Baltork, Iraj
• Format: Journal Article
• Published: 18.02.2022
• ISSN: 2046-2069
• DOI: 10.1039/d1ra08147k

The self-assembly approach was used for amine decoration of core/shell Fe 3 O 4 @Au with 4-aminothiophenol. This structure was used for covalent immobilization of lipase using a Ugi 4-component reaction. The amine group on the structure and carboxylic group from lipase can react in the Ugi reaction and a firm and stable covalent bond is created between enzyme and support. The synthesized structure was fully characterized and its activity was explored in different situations. The results showed the pH and temperature stability of immobilized lipase compared to free lipase in a wide range of pH and temperature. Also after 60 days, it showed excellent activity while residual activity for the free enzyme was only 10%. The synthesized structure was conveniently separated using an external magnetic field and reused 6 times without losing the activity of the immobilized enzyme. The self-assembly approach was used for amine decoration of core/shell Fe 3 O 4 @Au with 4-aminothiophenol.