Programmable Self-Assembly of DNA–Protein Hybrid Hydrogel for Enzyme Encapsulation with Enhanced Biological Stability

详细信息    查看全文

• 作者：Lan Wan ; Qiaoshu Chen ; Jianbo Liu ; Xiaohai Yang ; Jin Huang ; Li Li ; Xi Guo ; Jue Zhang ; Kemin Wang
• 刊名：Biomacromolecules
• 出版年：2016
• 出版时间：April 11, 2016
• 年：2016
• 卷：17
• 期：4
• 页码：1543-1550
• 全文大小：488K
• 年卷期：0
• ISSN：1526-4602

文摘

A DNA–protein hybrid hydrogel was constructed based on a programmable assembly approach, which served as a biomimetic physiologic matrix for efficient enzyme encapsulation. A dsDNA building block tailored with precise biotin residues was fabricated based on supersandwich hybridization, and then the addition of streptavidin triggered the formation of the DNA–protein hybrid hydrogel. The biocompatible hydrogel, which formed a flower-like porous structure that was 6.7 ± 2.1 μm in size, served as a reservoir system for enzyme encapsulation. Alcohol oxidase (AOx), which served as a representative enzyme, was encapsulated in the hybrid hydrogel using a synchronous assembly approach. The enzyme-encapsulated hydrogel was utilized to extend the duration time for ethanol removal in serum plasma and the enzyme retained 78% activity after incubation with human serum for 24 h. The DNA–protein hybrid hydrogel can mediate the intact immobilization on a streptavidin-modified and positively charged substrate, which is very beneficial to solid-phase biosensing applications. The hydrogel-encapsulated enzyme exhibited improved stability in the presence of various denaturants. For example, the encapsulated enzyme retained 60% activity after incubation at 55 °C for 30 min. The encapsulated enzyme also retains its total activity after five freeze–thaw cycles and even suspended in solution containing organic solvents.