交联和固定在聚丙烯微孔膜上后转谷氨酰胺酶形态和活性的变化。
Changes in morphology and activity of transglutaminase following cross-linking and immobilization on a polypropylene microporous membrane.
机构信息
Key Laboratory of Food Science and Engineering of Heilongjiang Province, Harbin University of Commerce, Harbin 150076, China.
出版信息
Molecules. 2011 Dec 5;16(12):10046-58. doi: 10.3390/molecules161210046.
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.
转谷氨酰胺酶（TGase）与戊二醛交联，通过紫外光接枝将交联结晶转谷氨酰胺酶固定在聚丙烯微孔膜上。固定化酶的活性计算为 0.128 U/cm²聚丙烯微孔膜。比较了游离、交联和固定化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适温度约为 40°C，而交联和固定化则分别提高到约 45°C 和 50°C。在 60°C 时，固定化、交联和游离转谷氨酰胺酶分别保留了 91.7±1.20%、63.2±1.05%和 37.9±0.98%的最大活性。转谷氨酰胺酶的最适 pH 不受其状态的影响。然而，交联和固定化转谷氨酰胺酶的热稳定性和 pH 稳定性都有所提高。
Zotero 插件