A novel type of hydrolase (BL28) from Bacillus licheniformis was identified, expressed in Escherichia coli, characterized, and immobilized for industrial applications. Biochemical characteristics of BL28 were investigated by performing SDS-PAGE, mass spectrometry, enzyme assays, CD spectroscopy, fluorescence, and in silico analysis. Using fluorescence microscopy, we investigated the effects of several chemical compounds on aggregate formation of BL28. Furthermore, cross-linked enzyme aggregates (CLEAs) of BL28 were prepared and scanning electron microscopy images were obtained. These CLEA-BL28 aggregates exhibited improved catalytic efficiencies and stabilities compared to free BL28 against harsh conditions of thermal or chemical stress. The characteristics of the CLEA-BL28 aggregates highlight their great potential in pharmaceutical and chemical industries.
