The aim of this work was to investigate the immobilization of the commercial Aspergillus
oryzae β-galactosidase enzyme (Deslac®) under different conditions, as well as to
characterize the free and immobilized enzyme using its application in lactose hydrolysis. The
experiments were conducted to identify the best yield of immobilization in calcium alginate
and the use of different adjuvants. The free and immobilized enzyme were characterized as to
their biochemical properties, to identify the optimum pH and temperature conditions for the
lactose hydrolysis reaction, the effect of salts on the enzymatic activity and enzyme storage
stability. Enzymes were analyzed to moisturize whey and whole milk. Immobilization of the
enzyme β-galactosidase yields better derivative inalginate (2% w/v), glutaraldehyde(25% v/v)
crosslinked pectin (2% w/v). The optimal pH to hydrolysis lactose using a soluble and
immobilized enzyme was 5.0 and 6.5, respectively, and the optimum temperature was 45 °C
and 40 °C, respectively. The use of magnesium sulfate and manganese sulfate influenced
enzymatic activity by 195% and 150%, respectively, for an immobilized enzyme. The
immobilized enzyme showed 60% stability after 10 days of storage. The immobilization
process with sodium alginate + pectin and glutaraldehyde reduced diffuse effects compared to
conventional alginate. The reduction of the temperature optimal activity allows a more
energy-efficient process.
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