文献类型：期刊文献

英文题名：Transglutaminase induced oligochitosan glycosylation of ferritin as a novel nanocarrier for food bioactive molecules

作者：Yang, Rui[1,2,3];Zuo, Peng[2];Zhang, Min[1];Meng, Demei[3];Wang, Baowei[4];Zhen, Tianyuan[4]

机构：[1]BTBU, Beijing Adv Innovat Ctr Food Nutr & Human Hlth, Beijing 100048, Peoples R China;[2]East China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai, Peoples R China;[3]Tianjin Univ Sci & Technol, State Key Lab Food Nutr & Safety, Tianjin 300457, Peoples R China;[4]Qingdao Agr Univ, Coll Food Sci & Engn, Qingdao 266109, Shandong, Peoples R China

年份：2019

卷号：94

起止页码：500

外文期刊名：FOOD HYDROCOLLOIDS

收录：;EI(收录号：20233314557335);WOS:【SCI-EXPANDED(收录号:WOS:000466780400051)】；

基金：This work was supported by the National Natural Science Foundation of China (No. 31501489), the Open Funding Project of the State Key Laboratory of Bioreactor Engineering, China, and the funding from Beijing Advanced Innovation Center for Food Nutrition and Human Health (No. 20171051), China.

语种：英文

外文关键词：Oligochitosan; Ferritin cage; Transglutaminase; Protein modification; Nanocarrier

摘要：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 rutinloaded 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.