Structural and functional characterization of kidney bean and field pea protein isolates: A comparative study
Structural and functional characterization of kidney bean and field pea protein isolates: A comparative study
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DOI：
10.1016/j.foodhyd.2014.07.024
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发表时间：
2015-01-01
影响因子：
10.7
通讯作者：
Rana, Jai Chand
中科院分区：
文献类型：
--
作者：
Shevkani, Khetan;Singh, Narpinder;Rana, Jai Chand
从不同的菜豆（KB）和豌豆（FP）品系制备蛋白分离物，并对其物理化学（蛋白含量、颜色、电泳图谱和zeta电位）、结构（热和构象）、动态流变学和功能（乳化、发泡、水和脂肪吸收）特性进行评价。这些分离物在颜色、结构、热和功能性质上存在显著差异。SDS-PAGE和大小排阻色谱显示，豌豆球蛋白（类似于150 kDa）是KB分离物中的主要蛋白质，而FP蛋白分离物含有豆球蛋白和豌豆球蛋白（类似于330和类似于155 kDa，分别）作为主要组分。红外光谱分析表明，KB和FP蛋白的二级结构主要为β折叠、β转角和α螺旋。KB蛋白具有相对较多的β-折叠（38.6%），而α-螺旋（22.8%）比FP蛋白（分别为30.0%和28.0%）。蛋白质分离物的流变学性质测量为凝胶化温度（T-gel）、凝胶增强（G（reinforcement））和tan δ。KB蛋白具有比FP蛋白更高的热变性温度（T-d）、T-gel和G（增强），而更低的tan δ。主成分分析（PCA）显示，T-d，T-gel和G（增强）呈正相关，而tan δ与β折叠的比例呈负相关。蛋白质溶解度、乳化稳定性、起泡性和稳定性与蛋白质上的电荷呈正相关。(C)2014爱思唯尔有限公司版权所有。
Protein isolates were prepared from different kidney bean (KB) and field pea (FP) lines and their physicochemical (protein content, colour, electrophoretic profile & zeta potential), structural (thermal & conformational), dynamic rheological and functional (emulsification, foaming, water and fat absorption) properties were evaluated. These isolates differed significantly in colour-, structural-, thermal-and functional-properties. SDS-PAGE and size exclusion chromatography revealed that vicilins (similar to 150 kDa) were prominent proteins in KB isolates, while FP protein isolates contained both legumins and vicilins (similar to 330 and similar to 155 kDa, respectively) as major components. FTIR spectroscopy revealed that beta-sheets, beta-turns and alpha-helix were main secondary structures in the KB and FP proteins. KB proteins had relatively more beta-sheets (38.6%) while less alpha-helix (22.8%) than FP proteins (30.0 and 28.0%, respectively). The rheological properties of the protein isolates were measured as gelation temperature (T-gel), gel reinforcement (G(reinforcement)) and tan delta. KB proteins had higher thermal denaturation temperature (T-d), T-gel and G(reinforcement) while lower tan delta than FP proteins. Principal component analysis (PCA) revealed that T-d, T-gel and G(reinforcement) related positively, whereas tan delta related negatively with the proportion of beta-sheets. Protein solubility, emulsion stability, foaming capacity and stability were positively related to the charge on the proteins. (C) 2014 Elsevier Ltd. All rights reserved.