The present study deals with the immobilization of Aspergillus oryzae galactosidase on concanavalin A layered Celite
545 as bioaffinity support. The activity yield of crosslinked enzyme was 71%. Michaelis constant, Km was 2.45 mM and
5.58 mM for soluble and crosslinked adsorbed galactosidase, respectively. Vmax for soluble and crosslinked adsorbed
enzyme was 0.52 mM/min and 0.38 mM/min, respectively. Moreover, Kiapp value of crosslinked galactosidase was
366
×
10−6 M while its soluble counterpart exhibited lower Kiapp value, 181
×
10−6 M at 2% galactose concentration. Soluble
and immobilized galactosidase exhibited same pH and temperature optima at pH 4.5 and 50 ◦C. The crosslinked
adsorbed enzyme retained 90% activity after 1 month of storage at 4 ◦C and 71% activity after its seventh repeated
use. Moreover, crosslinked galactosidase showed greater resistance to product inhibition mediated by glucose and
galactose. Crosslinked Con A-Celite adsorbed galactosidase showed increased efficiency in hydrolyzing lactose
from milk and whey in batch processes at 50 ◦C as compared to the adsorbed and soluble enzyme. The hydrolysis of
lactose in the continuous reactors containing crosslinked galactosidase was 92% and 81% at flow rate of 20 mL h−1
and 30 mL h−1 after 1 month of operation, respectively.