Study of microencapsulation of immunoglobulin Y on the targeted controlled intestinal release
文献类型: 外文期刊
作者: Lu, Wenjing 1 ; Chen, Di 1 ; Zhang, Cen 1 ; Ruan, Lingli 1 ; Zhang, Huajiang 3 ; Yao, Yunxin 4 ; Zhu, Dongrong 4 ; Xiao, Chaogeng 1 ;
作者机构: 1.Zhejiang Acad Agr Sci, Food Sci Inst, Zhejiang Key Lab Intelligent Food Logist & Proc, State Key Lab Managing Biot & Chem Threats Qual &, Hangzhou 310021, Peoples R China
2.Xishuangbanna Vocat & Tech Coll, Coll Food Sci & Technol, Xishuangbanna 666100, Peoples R China
3.Northeast Agr Univ, Fac Food Sci, Harbin 150030, Peoples R China
4.Zhejiang AGS Biotech Co Ltd, Huzhou 313100, Peoples R China
关键词: Egg yolk immunoglobulins; Shellac; Performance characterization; Release profile; Fourier transform infrared spectroscopy
期刊名称:LWT-FOOD SCIENCE AND TECHNOLOGY ( 影响因子:6.6; 五年影响因子:6.9 )
ISSN: 0023-6438
年卷期: 2025 年 218 卷
页码:
收录情况: SCI
摘要: Egg yolk immunoglobulin (IgY) is a highly active oral antibody closely related to human health. In order to maximize the retention of IgY's biological activity and improve its stability, shellac and lecithin were used as compound wall materials to embed IgY. An in vitro gastrointestinal digestion model and SDS-PAGE gel electrophoresis were used to evaluate the release profile of gel beads in the gastrointestinal tract. Simultaneously, enzyme linked immunosorbent assay (ELISA) was used to determine the activity of IgY within the gel beads. The interaction between core and wall materials was analyzed by fourier transform infrared spectroscopy (FTIR). The results showed that the gel beads exhibited optimal performance when the concentration of shellac was 15 g L-1, achieving an encapsulation efficiency of 85.9% and a loading capacity of 29.6% after embedding with the composite wall materials. Swelling release experiments and SDS-PAGE gel electrophoresis confirmed the in vitro release of IgY from the gel beads in the small intestine. FTIR analysis suggested that IgY underwent displacement of characteristic peaks due to possible electrostatic interactions. Overall, this study demonstrates that embedding IgY can effectively improve its stability, retain its activity, and potentially have applications in oral antibody delivery.
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