| 摘要: | 本研究旨在探討蔗糖分解酶 (Invertase, INV) 酵素固定化於鋁金屬基金屬有機骨架材料 (A520 和 Al-MIL-53) 上的應用，以優化轉化糖漿的生產。蔗糖分解酶能將蔗糖水解為葡萄糖和果糖，是製備轉化糖漿的重要催化劑。轉化糖漿 (Invert syrup) 因其較高的甜度和良好的保濕性，在食品工業中具有廣泛的應用，例如在烘焙和飲料行業中被廣泛使用。鋁金屬基金屬有機骨架材料 (Metal-organic Frameworks, MOFs)，如 A520 和 Al-MIL-53 ，因其高比表面積、可調控的孔徑和優異的穩定性，成為固定化酵素的理想載體。
本研究結果發現蔗糖分解酶固定化於 A520 和 Al-MIL-53 中，能顯著提高酵素的穩定性和活性。例如在反應溫度為 55°C 和 65°C 的高溫條件下將蔗糖分解酶包覆於 A520 材料中，其活性均較純蔗糖分解酶高出約 2 至 4 倍。這些 MOFs 材料能夠保護酵素在不利的反應條件（如高溫或強酸強鹼環境）下仍能保持其催化功能，從而提高反應效率和產品品質。此外，這種固定化方法還能有效防止酵素的溢漏問題，實現酵素的重複利用，降低生產成本。
未來的研究方向包括將酵素串聯反應（Tandem reactions）應用於固定化系統。例如，將 α-半乳糖苷酶（α-Galactosidase）和蔗糖分解酶聯合固定於 A520 和 Al-MIL-53 中，可實現棉子糖（Raffinose）一步轉化為高價值的轉化糖漿。此方法不僅簡化生產工藝，減少中間產物分離和酵素再利用步驟，還顯著提高生產效率和經濟效益。
綜上所述，本研究展示了 MOFs 在酵素固定化中的巨大潛力，為食品工業中的轉化糖漿生產提供高效且經濟的技術途徑。同時，這一技術在酵素串聯反應中的應用前景廣闊，有望實現多步驟反應的一體化操作，進一步提升工業生產效率和永續性。
;This study aims to investigate the application of invertase (INV) enzyme immobilization on aluminum-based metal-organic frameworks (MOFs), specifically A520 and Al-MIL-53, to optimize the production of invert syrup. Invertase catalyzes the hydrolysis of sucrose into glucose and fructose, serving as a crucial catalyst in the preparation of invert syrup. Due to its higher sweetness and excellent moisture retention properties, invert syrup is widely used in the food industry, particularly in baking and beverages. Aluminum-based MOFs, such as A520 and Al-MIL-53, are ideal carriers for enzyme immobilization due to their high specific surface area, tunable pore size, and exceptional stability.
The results of this study indicate that immobilizing invertase on A520 and Al-MIL-53 significantly enhances enzyme stability and activity. For instance, under high-temperature reaction conditions of 55°C and 65°C, invertase encapsulated in A520 material exhibited an activity approximately 2 to 4 times higher than that of pure invertase. These MOFs can protect the enzyme′s catalytic function under adverse reaction conditions, such as high temperatures or strong acidic and alkaline environments, thereby improving reaction efficiency and product quality. Additionally, this immobilization method effectively prevents enzyme leakage, enabling enzyme reuse and reducing production costs.
Future research directions include applying tandem reactions in immobilized systems. For example, co-immobilizing α-galactosidase and invertase on A520 and Al-MIL-53 could achieve the one-step conversion of raffinose to high-value invert syrup. This approach simplifies the production process, reduces intermediate product separation and enzyme reuse steps, and significantly enhances production efficiency and economic benefits.
In summary, this study demonstrates the significant potential of MOFs in enzyme immobilization, providing an efficient and economical technological approach for the production of invert syrup in the food industry. Moreover, this technology has broad application prospects in tandem enzyme reactions, potentially enabling the integration of multi-step reactions and further enhancing industrial production efficiency and sustainability. |
