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首页> 美国卫生研究院文献>Molecules >Changes in Morphology and Activity of Transglutaminase Following Cross-Linking and Immobilization on a Polypropylene Microporous Membrane
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Changes in Morphology and Activity of Transglutaminase Following Cross-Linking and Immobilization on a Polypropylene Microporous Membrane

机译：交联和固定在聚丙烯微孔膜上后谷氨酰胺转移酶的形态和活性的变化

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摘要

Transglutaminase (TGase) was cross-linked with glutaraldehyde, and cross-linked crystalline transglutaminase was immobilized on a polypropylene microporous membrane by UV-induced grafting. Immobilized enzyme activity were calculated to be 0.128 U/cm2 polypropylene microporous membrane. The microstructure and enzyme characteristics of free, cross-linked and immobilized transglutaminase were compared. The optimum temperature of free transglutaminase was determined to be approximately 40 °C, while cross-linking and immobilization resulted in an increase to approximately 45 °C and 50 °C. At 60 °C, immobilized, cross-linked and free transglutaminase retained 91.7 ± 1.20%, 63.2 ± 1.05% and 37.9 ± 0.98% maximum activity, respectively. The optimum pH was unaffected by the state of transglutaminase. However, the thermal and pH stabilities of cross-linked and immobilized transglutaminase were shown to increase.
机译：将转谷氨酰胺酶（TGase）与戊二醛交联，并通过紫外线诱导的接枝将交联的结晶转谷氨酰胺酶固定在聚丙烯微孔膜上。固定化酶活性计算为0.128 U / cm 2 聚丙烯微孔膜。比较了游离的，交联的和固定的转谷氨酰胺酶的微观结构和酶特性。游离转谷氨酰胺酶的最佳温度确定为约40°C，而交联和固定化导致温度升高到约45°C和50°C。在60°C下，固定化，交联和游离转谷氨酰胺酶的最大活性分别保持在91.7±1.20％，63.2±1.05％和37.9±0.98％。最佳pH不受转谷氨酰胺酶状态的影响。但是，交联的和固定的转谷氨酰胺酶的热稳定性和pH稳定性显示增加。

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