Improved radical scavenging activity of beta-lactoglobulin-xylobiose modified by the Maillard reaction
2007
Yajima, K.(Rakuno Gakuen Univ., Ebetsu, Hokkaido (Japan)) | Onodera, S. | Takeda, Y. | Kato, I. | Shiomi, N.
Beta-Lactoglobulin (beta-LG) was modified and conjugated to xylobiose using the Maillard reaction. The antioxidant activity of the Maillard reaction product, beta-LG-xylobiose, was measured in vtiro and compared to that of conjugated beta-LG-lactose. The reaction for 7 days led to conjugated beta-LG-xylobiose with a relative molecular mass ranging between 19 and 22 kDa based on SDS-PAGE analysis. It is confirmed that xylobiose bound to beta-LG by gas-liquid chromatography. One milligram of conjugated beta-LG-xylobiose contains 108 micro g of xylobiose, while the available epsilon-amino group content decreased to 40% after the Maillard reaction. Conjugated beta-LG-xylobiose had a higher radical scavenging activity than free beta-LG. As the modification by xylobiose had a higher efficiency than the modification by lactose, it is found that xylobiose is a useful oligosaccharide for protein modification. Furthermore, the radical scavenging activity of beta-LG was improved by modification with xylobiose.
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