Abstract
Numbers of reports have demonstrated the merits of confining enzyme in mesoporous supports, but have ignored the limitations to the application for biocatalytic transformation of a macrosubstrate. So in this work a strategy based on pH-triggered release and recovery of proteins has been presented to overcome this restriction. By modulation of the pH value, the encapsulated lysozyme was released from the mesopores to act on the macrosubstrate, displaying full bacteriolytic activity, and then was basically readsorbed by another pH modulation. The protein release-recovery is directly confirmed by confocal laser scanning microscopy (CLSM) and X-ray diffraction (XRD) observations. In virtue of substrate-enhanced desorption and privileged readsorption of lysozyme, high bioactivity and good reusability have been achieved.
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