Info

Estimated on the basis of the difference between the amount of protein applied and that remaining in supernatants and washings.

^Percentage of expressed activity (gel-bound activity/ applied activity).

Estimated on the basis of the difference between the amount of protein applied and that remaining in supernatants and washings.

^Percentage of expressed activity (gel-bound activity/ applied activity).

Enzyme Immobilization
Fig. 5. Kinetics for the immobilization of reduced K. lactis P-galactosidase onto thiol-reactive supports. ♦, TS-agarose; H,TSI-agarose; ▲, TSI-Toyopearl.

28. Nearly 70% of the total immobilized activity and 90% of the bound protein are eluted, showing the reversibility of the immobilization process.

29. The percentages of lactolysis (lactose hydrolysis) at 22°C are similar, regardless of the lactose solution (nearly 75% after 90 min of reaction).

30. When this mini-reactor is fed with whey permeate at 22°C, steady state lactose conversion reaches 90% and remains constant for 12 d. When it is fed for another 5 d with skimmed milk, the percentage of lactolysis is maintained.

31. After five cycles of 2.5 h each, the degree of lactolysis remains greater than 75%.

32. It is important to emphasize the differences found between TS- and TSI-gels from the point of view of regeneration. TSI-gels can be regenerated to 100% of their initial reactivity, whereas TS-gels can only be regenerated to 50% (Table 4).

Table 3

Stability of Immobilized P-Galactosidase Derivatives (Before and After Blocking With GSH) as a Function of the Incubation Period at 37°C.

Remaining activity (%) after incubation (h) Enzyme derivative 0.5 1 2

Table 3

Stability of Immobilized P-Galactosidase Derivatives (Before and After Blocking With GSH) as a Function of the Incubation Period at 37°C.

Remaining activity (%) after incubation (h) Enzyme derivative 0.5 1 2

TS-agarose-P-gal

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