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| Effects of D-galactosamine modification on structural properties and biological activities of zein |
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| KeyWord:zein D-galactosamine glycosylation structural property antioxidant activity |
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| Abstract: |
| With D-galactosamine containing primary amino groups as an acyl acceptor, zein was modified by glycosylation reaction catalyzed by transglutaminase(TGase). The effects of glycosylation modification on the structural properties and biological activities of zein were evaluated. The result of Fourier transform infrared spectra indicated that D-galactosamine covalently conjugated to the zein catalyzed by TGase. In the reaction system without D-galactosamine, the probability of cross-linked reaction of zein molecules catalyzed by TGase was low, and the cross-linked reaction had little effect on the structural properties of zein. Compared with original zein, the free sulfhydryl groups of the glycosylated zein decreased by 67.45 μmol/g, the denaturation temperature and the total denaturation enthalpy of the glycosylated zein increased by 8.8?℃ and 3197 J/g, respectively. These indicated that the thermal stability of zein was significantly improved by glycosylation. Meanwhile, antioxidant activities(including DPPH, superoxide anion, hydroxyl radical scavenging activities and reducing power) and alcohol dehydrogenase activation rate of the glycosylated zein increased significantly, which laid the theoretical foundation for further study on the hepatoprotective effects of the glycosylated zein. |
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