Solid State Fermentation of a Raw Starch Digesting Alkaline Alpha-Amylase from Bacillus licheniformis RT7PE1 and Its Characteristics.

Biotechnology Research International Pub Date : 2014-01-01 Epub Date: 2014-01-21 DOI:10.1155/2014/495384
Romana Tabassum, Shazia Khaliq, Muhammad Ibrahim Rajoka, Foster Agblevor
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引用次数: 14

Abstract

The thermodynamic and kinetic properties of solids state raw starch digesting alpha amylase from newly isolated Bacillus licheniformis RT7PE1 strain were studied. The kinetic values Q p , Y p/s , Y p/X , and q p were proved to be best with 15% wheat bran. The molecular weight of purified enzyme was 112 kDa. The apparent K m and V max values for starch were 3.4 mg mL(-1) and 19.5 IU mg(-1) protein, respectively. The optimum temperature and pH for α -amylase were 55°C, 9.8. The half-life of enzyme at 95°C was 17h. The activation and denaturation activation energies were 45.2 and 41.2 kJ mol(-1), respectively. Both enthalpies (ΔH (∗)) and entropies of activation (ΔS (∗)) for denaturation of α -amylase were lower than those reported for other thermostable α -amylases.

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地衣芽孢杆菌RT7PE1消化碱性α -淀粉酶的生淀粉固态发酵及其特性研究
研究了新分离的地衣芽孢杆菌RT7PE1菌株的固态原料淀粉消化α淀粉酶的热力学和动力学性质。在15%麦麸条件下,qp、yp /s、yp /X和qp的动力学值最好。纯化酶分子量为112 kDa。淀粉的表观K - m和V - max分别为3.4 mg mL(-1)和19.5 IU mg(-1)蛋白。α -淀粉酶最适温度为55℃,pH为9.8℃。酶在95℃时的半衰期为17h。活化活化能和变性活化能分别为45.2和41.2 kJ mol(-1)。α -淀粉酶变性的焓(ΔH(∗))和激活熵(ΔS(∗))均低于其他耐热性α -淀粉酶。
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