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- W2932615488 abstract "Abstract Ferritin is a cage-like protein with a modifiable exterior surface. In this study, transglutaminase was applied to catalyze the glycosylation of oligochitosan onto the apo-red bean seed ferritin (apoRBF) to fabricate an oligochitosan-modified apoRBF nanoparticle (OFN). Results indicated that the oligochitosan glycosylation retained the shell-like structure of ferritin and improved its thermal stability. The reversible assembly of OFN regulated by pH and urea transition was successfully retained. By using this assembly routine, rutin can be encapsulated within the OFN either by pH 2.0/7.0 transition or urea (8.0 M/0 M) transition, and the size distribution of rutin-loaded OFN was mainly about 12 nm. Moreover, the thermal stability of the rutin in the OFN was significantly improved as compared with that in apoRBF. The present study will be beneficial for extension of chitosan and Transglutaminase applications in protein modification, and will improve ferritin functionalization as a nanocarrier for food bioactive molecules." @default.
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- W2932615488 date "2019-09-01" @default.
- W2932615488 modified "2023-10-17" @default.
- W2932615488 title "Transglutaminase induced oligochitosan glycosylation of ferritin as a novel nanocarrier for food bioactive molecules" @default.
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- W2932615488 doi "https://doi.org/10.1016/j.foodhyd.2019.03.049" @default.
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