• Korean Journal of Food Science and Technology
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• v.20 no.4
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• pp.547-552
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• 1988

Aminoacylase immobilized on chitosan was applied for optical resolution of DL-amino acids. Optimun pH's for hydrolysis of N-ac DL Met, N-ac DL Try and N-ac DL Phe by immobilized aminoacylase were 8.0, 7.0, and 7.5, respectively. The pH stability of immobilized aminoacylase was less than that of soluble enzyme, while there was no difference in thermostability between immibilized and soluble enzymes. The reaction rate of immobilized enzyme was maximum, when concentrations of N-ac DL Met, N-ac DL Try and N-ac DL Phe were 0.05, 0.03 and 0.05M, respectively. Continuous resolution of M/20 N-ac DL amino acids with immobilized aminoacylase packed in a column resulted in 100% hydrolysis upto space velocity $2.0\;at\;45^{\circ}C$, and the half-life of the column at space velocity 5.0 was about 25 days. The yield of L-Met, L-Try and L-Phe recovered from 2 liter of column effluent were 57%, 52% and 52%, respectively.

• Korean Journal of Food Science and Technology
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• v.20 no.4
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• pp.541-546
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• 1988

Optimum conditions for immobilization of aminoacylase on chitosan were investigated, and the results are summerized as follows: Optimum conditions for activation of chitosan were pH 6.0, 0.2% of glutaraldehyde, and 120 minutes of reaction time. Enzyme concentration and reaction time for immobilization of aminoacylase on the activated chitosan were 80mg/20ml, and 90 minutes, respectively, and the yield of activity of the immobilized enzyme was 42.6%.