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Alcalase Enzymolysis of Red Bean (adzuki) Ferritin Achieves Nanoencapsulation of Food Nutrients in a Mild Condition
Journal of Agricultural and Food Chemistry ( IF 5.7 ) Pub Date : 2018-02-15 00:00:00 , DOI: 10.1021/acs.jafc.7b05656 Rui Yang 1, 2 , Yuqian Liu 1 , Demei Meng 1 , Christopher L. Blanchard 3 , Zhongkai Zhou 1
Journal of Agricultural and Food Chemistry ( IF 5.7 ) Pub Date : 2018-02-15 00:00:00 , DOI: 10.1021/acs.jafc.7b05656 Rui Yang 1, 2 , Yuqian Liu 1 , Demei Meng 1 , Christopher L. Blanchard 3 , Zhongkai Zhou 1
Affiliation
Classical methods to fabricate ferritin-nutrients shell–core nanoparticles usually apply extremely acid/alkaline pH transition, which may cause the activity loss of nutrients or the formation of insoluble aggregates. In this work, we prepared an extension peptide (EP) deleted red bean (adzuki) ferritin (apoRBFΔEP) by Alcalase 3.0T enzymolysis. Such enzymolysis could delete the EP domain and remain the typical shell-like structure of the ferritin. Meanwhile, the α-helix content of apoRBFΔEP was decreased by 5.5%, and the transition temperature (Tm) was decreased by 4.1 °C. Interestingly, the apoRBFΔEP can be disassembled into subunits under a benign condition at pH 4.0 and is assembled to form an intact cage protein when the pH was increased to 6.7. By using this novel route, the epigallocatechin gallate (EGCG) molecules were successfully encapsulated into the apoRBFΔEP cage with an encapsulation ratio of 11.6% (w/w), which was comparable with that by the traditional pH 2.0 transition. The newly prepared EGCG-loaded apoRBFΔEP exhibited a similarly protective effect on the EGCG upon simulated gastrointestinal tract and thermal treatment as compared with the control. In addition, the EGCG-loaded apoRBFΔEP could significantly relieve the ferritin association induced by pH transition, which was superior to traditional method. The thinking of this work will be especially suitable for encapsulating pH-sensitive molecules based on ferritin in a benign condition.
中文翻译:
红豆(碱性蛋白酶的酶解小豆)食品营养物质的铁达到纳米胶囊在温和的条件
制备铁蛋白营养素壳核纳米颗粒的经典方法通常会施加极强的酸/碱pH值过渡,这可能会导致营养素的活性丧失或形成不溶性聚集体。在这项工作中,我们制备了一个扩展的肽(EP)删除赤豆(小豆)铁蛋白(apoRBFΔ Ë P)由碱性蛋白酶酶解3.0T。这种酶解可以删除EP结构域,并保持铁蛋白的典型壳状结构。同时,apoRBFΔ的α螺旋含量Ê磷用5.5%降低,并且转变温度(Ť米)降低4.1℃。有趣的是,apoRBFΔ ê可以在pH 4.0的良性条件下将P分解为亚基,并在pH升高至6.7时组装成完整的笼状蛋白。通过使用这种新颖的途径,没食子儿茶素没食子酸酯(EGCG)的分子被成功地封装到apoRBFΔ ë P笼的11.6%的包封率(重量/重量),这是与由可比传统的pH为2.0的过渡。新制备的EGCG加载apoRBFΔ é作为与对照组相比P显示出对在模拟胃肠道和热处理的EGCG类似保护作用。此外,EGCG加载apoRBFΔ è磷可以显着缓解pH过渡诱导的铁蛋白缔合,优于传统方法。这项工作的思想将特别适合在良性条件下封装基于铁蛋白的pH敏感分子。
更新日期:2018-02-15
中文翻译:
红豆(碱性蛋白酶的酶解小豆)食品营养物质的铁达到纳米胶囊在温和的条件
制备铁蛋白营养素壳核纳米颗粒的经典方法通常会施加极强的酸/碱pH值过渡,这可能会导致营养素的活性丧失或形成不溶性聚集体。在这项工作中,我们制备了一个扩展的肽(EP)删除赤豆(小豆)铁蛋白(apoRBFΔ Ë P)由碱性蛋白酶酶解3.0T。这种酶解可以删除EP结构域,并保持铁蛋白的典型壳状结构。同时,apoRBFΔ的α螺旋含量Ê磷用5.5%降低,并且转变温度(Ť米)降低4.1℃。有趣的是,apoRBFΔ ê可以在pH 4.0的良性条件下将P分解为亚基,并在pH升高至6.7时组装成完整的笼状蛋白。通过使用这种新颖的途径,没食子儿茶素没食子酸酯(EGCG)的分子被成功地封装到apoRBFΔ ë P笼的11.6%的包封率(重量/重量),这是与由可比传统的pH为2.0的过渡。新制备的EGCG加载apoRBFΔ é作为与对照组相比P显示出对在模拟胃肠道和热处理的EGCG类似保护作用。此外,EGCG加载apoRBFΔ è磷可以显着缓解pH过渡诱导的铁蛋白缔合,优于传统方法。这项工作的思想将特别适合在良性条件下封装基于铁蛋白的pH敏感分子。