宫瑞林, 刘伯业, 陈复生, 王子祎. 小麦蛋白肽钙螯合物的制备工艺及结构表征[J]. 河南工业大学学报自然科学版, 2023, 44(6): 1-8,43. DOI: 10.16433/j.1673-2383.2023.06.001
    引用本文: 宫瑞林, 刘伯业, 陈复生, 王子祎. 小麦蛋白肽钙螯合物的制备工艺及结构表征[J]. 河南工业大学学报自然科学版, 2023, 44(6): 1-8,43. DOI: 10.16433/j.1673-2383.2023.06.001
    GONG Ruilin, LIU Boye, CHEN Fusheng, WANG Ziyi. Preparation and structural characterization of chelate of wheat protein peptide and calcium[J]. Journal of Henan University of Technology(Natural Science Edition), 2023, 44(6): 1-8,43. DOI: 10.16433/j.1673-2383.2023.06.001
    Citation: GONG Ruilin, LIU Boye, CHEN Fusheng, WANG Ziyi. Preparation and structural characterization of chelate of wheat protein peptide and calcium[J]. Journal of Henan University of Technology(Natural Science Edition), 2023, 44(6): 1-8,43. DOI: 10.16433/j.1673-2383.2023.06.001

    小麦蛋白肽钙螯合物的制备工艺及结构表征

    Preparation and structural characterization of chelate of wheat protein peptide and calcium

    • 摘要: 为开发新型的钙补充剂并拓宽小麦蛋白多肽的应用领域,对小麦蛋白制备多肽螯合钙的工艺及螯合物的特性进行研究。以小麦蛋白为原料、氯化钙为钙源,对比5种常见的商业酶和耐热蛋白酶PC 10F的水解效果及产生的活性肽对钙离子的螯合效果,利用单因素试验对制备工艺进行初步研究、正交试验进一步优化后,通过扫描电镜、紫外光谱、粒径电位对螯合物的结构进行表征。结果表明:水解度为6%时,耐热蛋白酶PC 10F酶解产生的多肽与钙离子螯合效果最佳;在反应温度50 ℃、多肽与氯化钙的质量比3∶1、时间50 min、反应体系pH 7的情况下,钙结合量可达60 mg/g以上。小麦蛋白多肽与CaCl2发生了螯合,螯合后的物质分子内部相互吸引发生聚集,致使其结构变得更加致密;多肽与钙离子配位结合形成环状结构,使得螯合物粒径变小,环状结构的生成导致螯合物更加稳定。

       

      Abstract: In order to develop a new type of calcium supplements and broaden the application field of wheat protein peptides, the preparation process of peptide-chelated calcium from wheat protein was explored and structural characterization was conducted. Using wheat protein as raw material and calcium chloride as calcium source, the hydrolysis effects of five common commercial enzymes and thermal protease PC 10F and the chelating effects of active peptides on calcium ions were compared. The preparation process was preliminarily studied by single factor test, and then further optimized by orthogonal test. The structure of the chelate was characterized by scanning electron microscopy, ultraviolet spectroscopy, and particle size potential. It was found that under the condition of 6% hydrolysis degree, the peptides produced by thermal protease PC 10F had the best chelating effect on calcium ions. The optimal process parameters were obtained when the reaction temperature was 50 ℃, the mass ratio of polypeptide to calcium chloride was 3∶1, the reaction time length was 50 min, and the reaction system pH value was 7. The binding amount of calcium with the chelates can reach higher than 60 mg/g. The chelating of wheat protein polypeptide and CaCl2 did occur, and a new substance was produced. After chelating, the internal molecules of the substance attracted to each other and aggregated, resulting in a more dense structure. The polypeptide and calcium ion coordinated to form a ring structure, resulting in a smaller size and a more stable state of the chelate. The wheat polypeptide chelated calcium obtained by the research has low production cost, simple process and practical application value.

       

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