Efficient Immobilization of Enzymes on Amino Functionalized MIL-125-NH2 Metal Organic Framework

As a series of metal organic framework (MOFs), materials of institute lavoisier frameworks (MILs) are expected to be excellent supports for enzyme immobilization due to their good water-stability and acid tolerance. However, enzyme loading on MIL-125-NH 2 is very low due to small pore size and few a...

Full description

Saved in:
Bibliographic Details
Published inBiotechnology and bioprocess engineering Vol. 27; no. 1; pp. 135 - 144
Main Authors Wang, Zichen, Liu, Yang, Li, Jinhong, Meng, Guoqing, Zhu, Daoyu, Cui, Jiandong, Jia, Shiru
Format Journal Article
LanguageEnglish
Published Seoul The Korean Society for Biotechnology and Bioengineering 01.02.2022
한국생물공학회
Subjects
acid tolerance
adsorption
ambient temperature
bioprocessing
Biotechnology
catalase
Chemistry
Chemistry and Materials Science
coordination polymers
immobilized enzymes
Industrial and Production Engineering
pH stability
porosity
Research Paper
thermal stability
생물공학
covalent binding
enzyme immobilization
MIL-125-NH
amino nationalization
Online AccessGet full text

Cover

More Information
Summary:As a series of metal organic framework (MOFs), materials of institute lavoisier frameworks (MILs) are expected to be excellent supports for enzyme immobilization due to their good water-stability and acid tolerance. However, enzyme loading on MIL-125-NH 2 is very low due to small pore size and few amino groups on the surface of the MIL-125-NH 2 . In this work, catalase (CAT) was immobilized on the MIL-125-NH 2 and amino functionalized MIL-125-NH 2 by adsorption (CAT@MIL-125-NH 2 ) and covalent binding (CAT@Amino MIL-125-NH 2 ), respectively. Compared with the CAT@MIL-125-NH 2 and free CAT, the CAT@Amino MIL-125-NH 2 displayed high activity recovery, good pH stability, stability against denaturants, and thermostability. Furthermore, activity recovery of CAT@Amino MIL-125-NH 2 was 56% higher than CAT@MIL-125-NH 2 . The CAT@Amino MIL-125-NH 2 still retained 50% residual activity for 14 days at room temperature, whereas free CAT lost activity after storage for 1 day at the same storage conditions. Furthermore, the CAT@Amino MIL-125-NH 2 maintained 62% of its initial activity after 4 consecutive uses, showing good reusability. The results showed that the amino functionalized MIL-125-NH 2 is an excellent carrier of enzyme immobilization.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1226-8372
1976-3816
DOI:10.1007/s12257-020-0393-y