• Korean Journal of Food Science and Technology
• /
• v.27 no.5
• /
• pp.753-756
• /
• 1995

Optimum conditions for immobilization of thermolysin, a metalloendopeptidase catalyzing synthesis of aspartame precursors, were investigated with using Amberlie XAD-7 as carrier and glutaraldehyde as cross-linking agent. Adsorption of thermolysin onto the carrier was rapid at the initial stage and 96% of the enzyme was adsorbed after 24 hours at $5^{\circ}C$. There was a linear relationship between amount of thermolysin adsorbed and thermolysin loaded upto 300g per liter of carrier. The effective range of cross-linking time, concentration of glutaraldehyde and pH for immobilization of the enzyme were $3{\sim}7\;hours,\;6{\sim}12.5%\;and\;pH\;6.0{\sim}7.0$, respectively. Degree of cross-linking and residual enzyme activity were high when cross-linked for 7 hours with 6% glutaraldehyde or for 3 hours with 12.5% glutaraldehyde. The residual enzyme activity was over 30% under these conditions.