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Immobilization of Bacillus licheniformis 5A1 milk-clotting enzyme andcharacterization of its enzyme properties

机译:地衣芽孢杆菌5A1凝乳酶的固定化及其酶学性质的表征

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摘要

Milk-clotting enzyme from Bacillus licheniformis 5A1 was immobilized on Amberlite IR-120 by ionic binding. Almost all the enzyme activity was retained on the support. The immobilized milk-clotting enzyme was repeatedly used to produce cheese in a batch reactor. The production of cheese was repeated 5 times with no loss of activity. The specific activity calculated on a bound-protein basis was slightly higher than that of free enzyme. The free and immobilized enzyme were highly tolerant to repeated freezing and thawing. The optimum temperature for milk-clotting activity was 70 pC with the free enzyme whereas, it was ranged from 70 to 80 pC with the immobilized milk-clotting enzyme. The activation energy (E A) of the immobilized milk-clotting enzyme was lower than the free enzyme (E A = 1.59 and 1.99 Kcal mol-p# respectively). The immobilized milk-clotting enzyme exhibited great thermal stability. The milk-clotting optimum pH was 7.0 for both free and immobilized enzyme. The Michaelis constant K m of the immobilized milk-clotting enzyme was slightly lower than the free enzyme.
机译:地衣芽孢杆菌5A1的凝乳酶通过离子结合固定在Amberlite IR-120上。几乎所有的酶活性都保留在载体上。固定的凝乳酶在间歇反应器中反复用于生产干酪。奶酪的生产重复了5次,没有活性降低。以结合蛋白为基础计算的比活性略高于游离酶。游离的固定化酶高度耐受反复冷冻和融化。游离酶的最佳凝乳活性温度为70 pC,而固定化凝乳酶的最佳温度为70至80 pC。固定化的牛奶凝结酶的活化能(E A)低于游离酶(E A分别为1.59和1.99 Kcal mol-p#)。固定化的牛奶凝结酶表现出很大的热稳定性。游离和固定化酶的凝乳最佳pH均为7.0。固定化牛奶凝结酶的米氏常数K m略低于游离酶。

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