Highly efficient solubilization of natural lignocellulosic materials by a commercial cellulase immobilized on various solid supports

Summary A commercial preparation of cellulase was immobilized on CNBr-sepharose, ConA-sepharose, and CNBr-glass beads. When filter paper was used as the substrate, the specific activity of the enzyme immobilized on ConA-sepharose was more than twice that of the soluble enzyme, while the activity of the enzymes immobilized on the other two substrates was either very slightly (CNBr-sepharose) or slightly (CNBr-glass beads) reduced. The immobilized enzymes showed alterations both in the Km and V max values: these were generally either slightly increased (Km) or reduced (V max). In addition, the immobilized enzymes were more resistant to inhibition both by glucose and cellobiose, they were all more stable than the soluble enzyme and solubilized three different natural lignocellulosic materials (alfa-alfa, wheat straw, and pine needles) to a much greater or significantly greater extext than the soluble enzyme: the ConA-sepharose cellulase was the most efficient. The possibility of reusing the immobilized enzyme was also tested. It was found that the ConA-sepharose cellulase could be reused five times with a final loss of activity that ranged between 30% and 50%.     

Procoagulant activity of mouse transformed cells: Different expression in freshly isolated or cultured cells

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