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Encapsulation of Spherical Cross-Linked Phenylalanine Ammonia Lyase Aggregates in Mesoporous Biosilica
- Cui, Jiandong, Zhao, Yamin, Feng, Yuxiao, Lin, Tao, Zhong, Cheng, Tan, Zhilei, Jia, Shiru
- Journal of agricultural and food chemistry 2017 v.65 no.3 pp. 618-625
- biomimetics, calcium carbonate, catalytic activity, crosslinking, encapsulation, immobilized enzymes, mass transfer, mineralization, phenylalanine ammonia-lyase, porous media, thermal stability
- Cross-linked enzyme aggregates (CLEAs) have recently emerged as a promising tool for enzyme immobilization because of their simplicity and low cost. However, a lack of good size and morphological control over the as-prepared CLEAs has limited their practical applications. For example, the prepared CLEAs exhibit amorphous large clusters that would cause significant mass-transfer limitations, which lead to a low catalytic efficiency. Here, inspired by biomineralized core–shell structures in nature, we develop a novel mesoporous spherical CLEA with a biosilica shell by using phenylalanine ammonia lyase based on CaCO₃ microtemplates and biomimetic mineralization. The resultant CLEAs exhibited a spherical structure with good monodispersity instead of the amorphous clusters of conventional CLEAs and showed activity higher than that of conventional CLEAs. Moreover, the thermostability, tolerance against denaturants, and mechanical stability of the spherical CLEAs with a biosilica shell were enhanced significantly compared with those of conventional CLEAs. In particular, the spherical CLEAs with a biosilica shell retained 70% of their original activity after 13 cycles, whereas the conventional CLEAs retained only 35% of their original activity. This approach could be an efficient strategy for improving the catalytic properties of CLEAs.