Enzyme promotes the hydrogelation from a hydrophobic small molecule.
We report in this paper that an enzymatic reaction can be used as the sole mechanism for forming supramolecular hydrogels that have good stability in aqueous solutions at room temperature. The gels are two-component hydrogels that are mainly formed by hydrophobic compound 2 and doped with hydrophilic compound 1. They were formed by an enzymatic process that produces hydrophobic 2 in homogeneous modes and assists the formation of three-dimensional networks. We have characterized the morphologies of the gels with scanning electron microscopy and dark-field transmission electron microscopy, collected fluorescence data to monitor the gelation process, and proposed a possible mechanism to explain the formation of the gels.
Gao
Jie
J
Key Laboratory of Bioactive Materials, Ministry of Education, Tianjin 300071, PR China.
Wang
Huaimin
H
Wang
Ling
L
Wang
Jingyu
J
Kong
Deling
D
Yang
Zhimou
Z
D055162:Biocatalysis; D020100:Hydrogels / Q000737:chemistry* / Q000378:metabolism*; D057927:Hydrophobic and Hydrophilic Interactions; D008855:Microscopy, Electron, Scanning; D008856:Microscopy, Fluorescence; D008958:Models, Molecular; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*
D020100:Hydrogels; D010744:Phosphoric Monoester Hydrolases