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The Increase of thermal stability of a-amylase from locale bacteria Isolate Sac/7/t/s subtilis ITBCCB148 by chemical modification with dimethyladipimidate

机译:通过用二甲基己二酸二甲酯进行化学修饰,提高局部细菌中α-淀粉酶的热稳定性,分离出Sac / 7 / t / s枯草杆菌ITBCCB148

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The attempt to increase thermal stability of alpha-amylase from local bacteria isolate Bacillus subtilis ITBCCB148 was performed by chemical modification using dimethyladipimidate (DMA). The results showed that the native and modified enzymes with DMA(0.3%; 0.5%; and 0.7%) have a similar optimum temperature of 60deg C. The thermal stability test done to the native and modified enzymes at 60deg C and 60 minutes showed that the native enzyme have a residual activity of 7.7% and t_1,2 of 15.4 min, while t_1/2 0f the modified enzymes were 23.9,43.3 and 53.3 min. with residual activity of 15.9%, 35.5%, and 42.5, respectively The chemical modification with DMA to alpha-amylase has shown to increase the thermal stability of the enzyme between 1.5 - 3.5 times compared to that of the native enzyme.
机译:尝试通过使用二甲基己二酸二甲酯(DMA)进行化学修饰来提高来自本地细菌分离株枯草芽孢杆菌ITBCCB148的α-淀粉酶的热稳定性。结果表明,具有DMA(0.3%; 0.5%;和0.7%)的天然酶和修饰酶的最佳温度相似,为60℃。在60℃和60分钟时对天然酶和修饰酶进行的热稳定性测试表明:天然酶的残留活性为7.7%,t_1,2的剩余活性为15.4 min,而t_1 / 2 0f的修饰酶为23.9、43.3和53.3 min。分别具有15.9%,35.5%和42.5的残留活性。用DMA对α-淀粉酶进行的化学修饰显示,与天然酶相比,该酶的热稳定性提高了1.5-3.5倍。

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