Thermostability of yeast lactase (Kluyveromyces marxianus) in milk

Abstract

SummaryThe half-life (∼ 2 h) of commercial yeast lactase (Kluyveromyces marxianus) in milk at 45 °C was 20 times greater than in milk salts and 50 times greater than in phosphate buffer. K was a more effective stabilizer than Na, both in milk salts and buffer. Stability was markedly reduced by the absence of divalent cations. Lactose and caseinate both stabilized the enzyme about 5-fold in milk salts, but together they stabilized it almost 50-fold. At equimolar concentrations, galactose was almost as effective as lactose as a stabilizer, but glucose was much less effective and sucrose had no effect. Stability in milk was independent of enzyme concentration, but varied with concentration of milk solids, reaching a maximum at about 25% solids. In milk, enzyme denaturation was more sensitive to changes in temperature in the range 42–53 °C than in the range 30–40 °C. At a concentration of 10O-nitrophenyl-β-d-galactopyranoside units/ml it took 19 min at 45 °C to achieve 80% hydrolysis of lactose in milk, compared to 87 min at 30 °C.