Abstract
A novel enzyme immobilization approach was used to generate mesoporous enzymes-silica composite microparticles by co-entrapping gelatinized starch and cross-linked phenylalanine ammonia lyase (PAL) aggregates (CLEAs) containing gelatinized starch into biomemitic silica and subsequently removing the starch by α-amylase treatment. During the preparation process, the gelatinzed starch served as a pore-forming agent to create pores in CLEAs and biomimetic silica. The resulting mesoporous CLEAs-silica composite microparticles exhibited higher activity and stability than native PAL, conventional CLEAs, and PAL encapsulated in biomimetic silica. Furthermore, the mesoporous CLEAs-silica composite microparticles displayed good reusability due to its suitable size and mechanical properties, and had excellent stability for storage. The superior catalytic performances were attributed to the combinational unique structure from the intra-cross-linking among enzyme aggregates and hard mesoporous silica shell, which not only decreased the enzyme-support negative interaction and mass-transfer limitations, but also improved the mechanical properties and monodispersity. This approach will be highly beneficial for preparing various bioactive mesoporous composites with excellent catalytic performance.
Highlights
A novel enzyme immobilization approach was used to generate mesoporous enzymes-silica composite microparticles by co-entrapping gelatinized starch and cross-linked phenylalanine ammonia lyase (PAL) aggregates (CLEAs) containing gelatinized starch into biomemitic silica and subsequently removing the starch by α-amylase treatment
To address the limitations associated with current immobilization technology, we utilized phenylalanine ammonia lyase (PAL) from Rhodotorula glutinis (R. glutinis) as a model system, and reported a simple approach to preparing novel mesoporous cross-linked enzyme aggregates (CLEAs)-silica composite microparticles (P-CLEAs-Si)
The starch in CLEAs and biomimetic silica was removed by adding α -amylase to form mesoporous CLEAs-silica composite microparticles
Summary
A novel enzyme immobilization approach was used to generate mesoporous enzymes-silica composite microparticles by co-entrapping gelatinized starch and cross-linked phenylalanine ammonia lyase (PAL) aggregates (CLEAs) containing gelatinized starch into biomemitic silica and subsequently removing the starch by α-amylase treatment. The increased tolerance towards high temperature, extreme pH and chemical denaturants for P-CLEAs-Si may be due to the following reasons: (1) entrapment of water molecules in the biomimetic silica could help enzyme retain its structure and function; (2) the silica shell may provide a suitable microenvironment to reduce the deformation of PAL structures at high temperatures, extreme pH, and under harsh denaturants due to the retard of heat transfer and the denaturant corrosion[32]; (3) intra-cross-linking among enzyme aggregates improved the rigidity of the active conformation.
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