Rocha Gabriela Fernanda, Kise Francisco, Rosso Adriana Mabel, Parisi Mónica Graciela
Laboratorio de Química Biológica, Departamento de Ciencias Básicas-Universidad Nacional de Luján. Ruta 5 y Avenida Constitución, Luján, 6700 Buenos Aires, Argentina.
Laboratorio de Química Biológica, Departamento de Ciencias Básicas-Universidad Nacional de Luján. Ruta 5 y Avenida Constitución, Luján, 6700 Buenos Aires, Argentina.
Food Chem. 2017 Dec 15;237:350-355. doi: 10.1016/j.foodchem.2017.05.112. Epub 2017 May 23.
An aspartic protease from Salpichroa origanifolia fruits was successfully immobilized onto an activated support of glutaraldehyde agarose. The immobilized enzyme presented higher thermal stability than the free enzyme from 40°C to 50°C and high reusability, retaining 54% of the initial activity after ten cycles of the process. Whey protein concentrates (WPC) were hydrolyzed with both free and immobilized enzyme, reaching a similar degree of hydrolysis of approximately 6-8% after 20h. In addition, the immobilized derivate hydrolyzed α-lactalbumin protein with a higher affinity than β-lactoglobulin. The hydrolysate was ultra-filtrated, and the fractions were evaluated for antioxidant activities with the 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity method. The fraction containing peptides with a molecular mass below 3kDa demonstrated a strong radical quenching effect (IC 0.48mg/ml). These results suggest that hydrolyzed WPC could be considered as a promising source of natural food antioxidants for the development of functional food.
一种来自牛心番荔枝果实的天冬氨酸蛋白酶成功固定在戊二醛琼脂糖活化载体上。固定化酶在40°C至50°C范围内比游离酶具有更高的热稳定性和高重复使用性，在该过程的十个循环后仍保留54%的初始活性。用游离酶和固定化酶水解乳清浓缩蛋白（WPC），20小时后达到相似的水解程度，约为6 - 8%。此外，固定化衍生物水解α-乳白蛋白的亲和力高于β-乳球蛋白。对水解产物进行超滤，并用2,2-二苯基-1-苦基肼基（DPPH）自由基清除活性法评估各组分的抗氧化活性。分子量低于3kDa的含肽组分表现出强烈的自由基猝灭作用（IC 0.48mg/ml）。这些结果表明，水解的WPC可被视为开发功能性食品的天然食品抗氧化剂的有前途的来源。
