Biomimetic immobilization of α-glucosidase inspired by antibody-antigen specific recognition for catalytic preparation of 4-methylumbelliferone

Shuang Guo; Shuo Liu; Chang Liu; Yi Wang; Dongyu Gu; Jing Tian; Yi Yang

doi:10.1016/j.ijbiomac.2024.131697

Biomimetic immobilization of α-glucosidase inspired by antibody-antigen specific recognition for catalytic preparation of 4-methylumbelliferone

Int J Biol Macromol. 2024 Apr 28;268(Pt 2):131697. doi: 10.1016/j.ijbiomac.2024.131697. Online ahead of print.

Authors

Shuang Guo¹, Shuo Liu¹, Chang Liu², Yi Wang², Dongyu Gu³, Jing Tian⁴, Yi Yang⁵

Affiliations

¹ School of Light Industry and Chemical Engineering, Dalian Polytechnic University, Dalian 116034, China.
² School of Biological Engineering, Dalian Polytechnic University, Dalian 116034, China.
³ College of Marine Science and Environment, Dalian Ocean University, Dalian 116023, China. Electronic address: gudongyu@dlou.edu.cn.
⁴ School of Biological Engineering, Dalian Polytechnic University, Dalian 116034, China. Electronic address: tianjing@dlpu.edu.cn.
⁵ School of Light Industry and Chemical Engineering, Dalian Polytechnic University, Dalian 116034, China. Electronic address: yangyi105@mails.ucas.ac.cn.

PMID: 38688333
DOI: 10.1016/j.ijbiomac.2024.131697

Abstract

Immobilization technology plays an important role in enhancing enzyme stability and environmental adaptability. Despite its rapid development, this technology still encounters many challenges such as enzyme leakage, difficulties in large-scale implementation, and limited reusability. Drawing inspiration from natural paired molecules, this study aimed to establish a method for immobilized α-glucosidase using artificial antibody-antigen interaction. The proposed method consists of three main parts: synthesis of artificial antibodies, synthesis of artificial antigens, and assembly of the artificial antibody-antigen complex. The critical step in this method involves selecting a pair of structurally similar compounds: catechol as a template for preparing artificial antibodies and protocatechualdehyde for modifying the enzyme to create the artificial antigens. By utilizing the same functional groups in these compounds, specific recognition of the antigen by the artificial antibody can be achieved, thereby immobilizing the enzymes. The results demonstrated that the immobilization amount, specific activity, and enzyme activity of the immobilized α-glucosidase were 25.09 ± 0.10 mg/g, 5.71 ± 0.17 U/mg_protein and 143.25 ± 1.71 U/g_carrier, respectively. The immobilized α-glucosidase not only exhibited excellent reusability but also demonstrated remarkable performance in catalyzing the hydrolysis of 4-methylumbelliferyl-α-D-glucopyranoside.

Keywords: Artificial antibody-antigen; Enzyme immobilization; α-Glucosidase.