From　the　aqueous　extract　of　Semen　Armeniacae　Amarum,　a　major　protein　isolate　was　purified　and　characterized　as　a　novel　member　of　the　11S　globulin　family,　which　is　composed　of　three　polypeptides　linked　by　disulfide　bond.　Furthermore,　the　feasibility　of　using　the　isolated　protein　for　fabricating　nanocarriers　was　investigated.　The　results　indicate　that　thermal　treatment　of　the　globulin　induced　the　rearrangement　of　the　disulfide　bond　to　form　homodimers　of　acid　polypeptides　during　the　formation　of　nanoparticles.　The　harvested　nanoparticles　produced　by　heat-induced　assembly　are　spherical　in　shape,　with　an　average　size　of　92　nm　and　exhibited　low　cytotoxicity　to　L-02　and　MDCK　cell　lines.　These　nanoparticles　are　capable　to　encapsulate　paclitaxel,　estimated　the　maximum　encapsulation　efficiency　of　paclitaxel　loaded　to　the　nanoparticles　was　92.6%　and　the　maximum　release　of　paclitaxel　was　57.4%.　This　research　suggests　that　the　screening　of　traditional　herbal　extracts　could　provide　a　novel　source　of　protein　nanocarriers.　©　2020　Elsevier　B.V.