Purified pectin lyase from Bacillus cereus was successfully immobilized in alginate beads with a high binding efficiency of 84.55%. The optimal immobilization was achieved using 2.5% (w/v) alginate concentration. Both free and immobilized enzyme showed optimum pH of 10.0 and temperatures of 40 and 45°C respectively. Pectin lyase gave maximum activity at a substrate concentration of 0.5% w/v for free and 0.75% w/v for the immobilized enzyme and relatively similar V_max values were obtained for both free (3.3 µmol/min) and immobilized pectin lyase (3.6 µmol/min). The K_m for the immobilized pectin lyase (0.19 mg/ml) was slightly higher than that of the free (0.16 mg/ml) enzyme. The maximum inhibition of 50.2% was observed in the presence of Hg²⁺ ion for free pectin lyase and immobilized enzyme showed maximum inhibition of 67.32% in the presence of Na⁺ ion with statistically significant p-value (p < 0.05). Thermal stability was not significantly altered by immobilization. Thermal stability of free and immobilized pectin lyase was relatively similar at different temperatures. The immobilized pectin lyase retained almost 53% of its original activity up to 7^th cycle. Furthermore, during storage at 4°C, immobilized pectin lyase retained relative activity of 79.77% and free enzyme retained 63.63% relative activity upto 35 days of storage, this indicated that the immobilization improved stability of the enzyme.

中文翻译：

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蜡状芽孢杆菌游离和藻酸钙固定化碱性果胶裂解酶的理化特性

来自蜡样芽孢杆菌的纯化的果胶裂解酶已成功固定在藻酸盐珠粒中，具有84.55％的高结合效率。使用2.5％（w / v）藻酸盐浓度可实现最佳固定。游离和固定化酶的最佳pH分别为10.0，温度分别为40和45°C。果胶裂解酶在游离底物浓度为0.5％w / v和固定酶为0.75％w / v的底物浓度下具有最大活性，并且游离（3.3 µmol / min）和固定果胶裂解酶（3.6）均获得相对相似的V _max值。 µmol / min）。该ķ_米固定化果胶裂解酶（0.19 mg / ml）的酶解速率略高于游离酶（0.16 mg / ml）。在Hg ²⁺离子存在下，对果胶裂解酶的最大抑制作用为50.2％，在Na ⁺离子存在下，固定化酶的最大抑制作用为67.32％，p值具有统计学意义（p <0.05）。固定化不会明显改变热稳定性。游离和固定的果胶裂解酶在不同温度下的热稳定性相对相似。固定的果胶裂解酶保留了其最初活性的几乎53％，直至^第7天周期。此外，在4°C下储存期间，固定化的果胶裂解酶保留相对活性为79.77％，游离酶保留相对活性为63.63％，直至储存35天，这表明固定化提高了酶的稳定性。