Improvement of thermal stability of β-galactosidase from Bacillus circulans by multipoint covalent immobilization in hierarchical macro-mesoporous silica
C Bernal, L Sierra, M Mesa - Journal of Molecular Catalysis B: Enzymatic, 2012 - Elsevier
β-Galactosidase from Bacillus circulans was immobilized on hierarchical macro-
mesoporous silica by multipoint covalent attachment by formation of Schiff bases between
enzyme and support. The enzyme was effectively immobilized with high yields (around 60–
80%) and expressed activity (around 50–80%) depending on the concentration of aldehyde
groups in the carrier. Immobilization of β-galactosidase in chemically modified silica
conferred excellent thermal stability to the biocatalyst and enzyme leaching was completely …
mesoporous silica by multipoint covalent attachment by formation of Schiff bases between
enzyme and support. The enzyme was effectively immobilized with high yields (around 60–
80%) and expressed activity (around 50–80%) depending on the concentration of aldehyde
groups in the carrier. Immobilization of β-galactosidase in chemically modified silica
conferred excellent thermal stability to the biocatalyst and enzyme leaching was completely …
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