Changes in morphology and activity of transglutaminase following cross-linking and immobilization on a polypropylene microporous membrane |
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Authors: | Shi Yan-Guo Qian Lei Zhang Na Han Chun-Ran Liu Ying Zhang Yi-Fang Ma Yong-Qiang |
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Institution: | Key Laboratory of Food Science and Engineering of Heilongjiang Province, Harbin University of Commerce, Harbin 150076, China. |
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Abstract: | 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. |
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