Univ. Montpellier, INRAE, Institut Agro, UMR IATE, Montpellier, France; INRAE, UR BIA, Rue Yvette Cauchois, F-44316 Nantes, France.
Univ. Montpellier, INRAE, Institut Agro, UMR IATE, Montpellier, France.
Food Chem. 2022 Jul 1;381:132254. doi: 10.1016/j.foodchem.2022.132254. Epub 2022 Jan 29.
This study provides a detailed characterisation of a leaf protein concentrate (LPC) extracted from Cichorium endivia leaves using a pilot scale process. This concentrate contains 74.1% protein and is mainly composed of Ribulose-1,5-BISphosphate Carboxylase/Oxygenase (RuBisCO). We show that the experimentally determined extinction coefficient (around 5.0 cm g L depending on the pH) and refractive index increment (between 0.27 and 0.39 mL g) are higher than the predicted ones (about 1.6 cm g L and 0.19 mL g, respectively). In addition, the UV-visible absorption spectra show a maximum at 258 nm. These data suggest the presence of non-protein UV-absorbing species. Chromatographic separation of the concentrate components in denaturing conditions suggests that RuBisCO SC may be covalently bounded to few phenolic compounds. Besides, the solubility of LPC proteins is higher than 90% above pH 6. Such high solubility could make LPC a good candidate as a functional food ingredient.
本研究使用中试规模的工艺，详细描述了从菊苣叶中提取的叶蛋白浓缩物（LPC）。该浓缩物含有 74.1%的蛋白质，主要由核酮糖-1,5-二磷酸羧化酶/加氧酶（RuBisCO）组成。我们发现，实验测定的消光系数（取决于 pH 值，约为 5.0 cm g L）和折射率增量（0.27 至 0.39 mL g 之间）均高于预测值（约 1.6 cm g L 和 0.19 mL g）。此外，紫外-可见吸收光谱在 258 nm 处显示出最大值。这些数据表明存在非蛋白质的紫外吸收物质。在变性条件下对浓缩物成分进行色谱分离表明，RuBisCO SC 可能与少数酚类化合物发生共价结合。此外，LPC 蛋白的溶解度在 pH 值高于 6 时高于 90%。如此高的溶解度使 LPC 成为功能性食品成分的良好候选物。
