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中国精品科技期刊2020

大豆分离蛋白-阿拉伯糖美拉德反应产物对α-淀粉酶抑制剂微囊化特性研究

Microencapsulation Properties of α-Amylase Inhibitors with Soy Protein Isolate-Arabinose Maillard Reaction Products

  • 摘要: 为提高α-淀粉酶抑制剂在加工与应用过程中的稳定性,本研究以大豆分离蛋白–阿拉伯糖混合物及其美拉德反应产物为基础,与海藻酸钠复合构建壁材,用于制备α-淀粉酶抑制剂微胶囊。系统表征了复合壁材的理化性质,并比较了不同微胶囊的形貌与稳定性,以阐明微囊化对活性成分的保护机制及美拉德反应产物作为壁材的优势。结果显示,美拉德反应产物显著提高了α-淀粉酶抑制剂在微胶囊中的稳定性和活性保留率。该微胶囊包埋率达91.57%,α-淀粉酶抑制剂含量达170.01 mg/g,平均粒径为1229.50 μm,呈均一颗粒状,均显著优于未发生美拉德反应的微胶囊。此外,这类微胶囊在高温(≥70 ℃)、酸性或碱性条件(pH≤4或pH≥8)及模拟胃液环境下均表现出更优的稳定性。综上所述,美拉德反应产物作为微胶囊壁材可显著提升α-淀粉酶抑制剂的加工适应性和生物利用度。本研究为α-淀粉酶抑制剂的进一步开发及功能性食品的研发提供了新的思路和理论依据。

     

    Abstract: To enhance the stability of α-amylase inhibitors throughout processing and application, soybean protein isolate-arabinose mixtures and their Maillard reaction products were employed as composite wall materials in conjunction with sodium alginate to fabricate α-amylase inhibitor microcapsules. The physicochemical characteristics of the composite wall systems were systematically investigated, while the morphology and stability of the resulting microcapsules were comparatively evaluated, thereby elucidating the protective mechanism of microencapsulation and highlighting the advantages of Maillard reaction products as wall materials. The results demonstrated that incorporation of Maillard reaction products markedly improved the stability and activity retention of α-amylase inhibitors within the microcapsules. The optimized formulation achieved an encapsulation efficiency of 91.57%, an α-amylase inhibitor content of 170.01 mg/g, and an average particle size of 1229.50 μm, exhibiting uniform and well-defined spherical morphology, all of which were significantly superior to those of microcapsules prepared without Maillard modification. Moreover, the Maillard-based microcapsules displayed enhanced stability under elevated temperatures (≥70 ℃), extreme pH conditions (pH ≤4 or pH ≥8), as well as in simulated gastric fluid. Collectively, these findings indicate that Maillard reaction products function as effective wall materials for microencapsulation, substantially improving the processing adaptability and bioavailability of α-amylase inhibitors and offering a promising strategy for their further development and application in functional foods.

     

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