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首页> 外文期刊>African Journal of Biotechnology >Immobilization of raw starch digesting amylase on silica gel: A comparative study
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Immobilization of raw starch digesting amylase on silica gel: A comparative study

机译：在硅胶上固定淀粉消化淀粉酶的固定化：比较研究

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To stabilize the raw starch digesting amylase from fungus?Aspergillus carbonarius(Bainier) Thom IMI 366159, the enzyme was immobilized on an inorganic porous support silica gel using different methods. Immobilization was carried out by spontaneous adsorption and crosslinking (reticulation), initial physical adsorption followed by crosslinking or conjugation on a silica gel activated with glutaraldehyde or polyglutaraldehyde. Concentration of glutaraldehyde, pH and duration of enzyme immobilization greatly influenced immobilization yield. A shift of optimum pH from pH 5 to 6 was observed for reticulated raw starch digesting amylase (RSDA), while other immobilized derivatives remained the same as the soluble enzyme. Immobilized enzyme exhibited increased activity at alkaline pH 8 to 9. Glutaraldehyde and polyglutaraldehyde activated RSDA showed lower activity at acidic pH 3.5 to 4 as compared to the crosslinked enzyme derivatives which had above 75% activity. The temperature optimum for the reticulated derivative was remarkably broadened from 30 to 60°C. All immobilized derivatives were more active and stable at higher temperatures to varying degrees. Soluble amylase lost 30% of its activity after 2 h incubation at 65°C, while 2.9% loss was recorded for reticulated derivative, 6.2% loss was recorded for physically adsorbed and crosslinked derivative, and 1.9 and 10% loss was recorded for polyglutaraldehyde and glutaraldehyde activated derivatives, respectively. Immobilization led to a slight decrease in?Km?for all the derivatives. However, spontaneous adsorption and crosslinking (reticulation) of RSDA to silica gel with glutaraldehyde gave the best overall stability results.
机译：为了使原料淀粉消化淀粉酶从真菌稳定β-曲霉（Bainier）Thom IMI 366159，将酶固定在无机多孔载体硅胶上使用不同的方法。通过自发吸附和交联（近奇化），初始物理吸附，然后在用戊二醛或聚戊二醛活化的硅胶上交联或缀合进行固定。戊二醛浓度，pH和酶固定持续时间大大影响了固定产量。对于网状原料淀粉消化淀粉酶（RSDA），观察到最佳pH从pH5至6的偏移，而其他固定化衍生物保持与可溶性酶相同。固定化酶在碱性pH 8至9上表现出增加的活性。与具有高于75％活性的交联酶衍生物相比，戊二醛活化RSDA在酸性pH 3.5至4中显示出较低的活性。用于网状衍生物的温度从30至60℃显着宽。所有固定化衍生物在更高的温度下更活跃，稳定到不同程度。在65℃的温育后，可溶性淀粉酶损失了30％的活性，而记录了2.9％的损失以进行网状衍生物，记录有6.2％的损失，用于物理吸附和交联的衍生物，并记录为聚谷氨酸的1.9％和10％的损失。戊二醛活化衍生物分别。固定化导致稍微减少？KM？对于所有衍生物。然而，用戊二醛对硅胶的自发吸附和交联（网状化）对谷氨酸的硅胶产生了最佳的整体稳定性结果。

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