Comparison of protein chemical and physicochemical properties of rapeseed cruciferin with those of soybean glycinin.
Comparison of protein chemical and physicochemical properties of rapeseed cruciferin with those of soybean glycinin.
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油菜十字花科素与大豆甘氨酸的蛋白质化学和理化性质比较。
DOI：
10.1021/jf0202537
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发表时间：
2002
影响因子：
6.1
通讯作者：
S. Utsumi
中科院分区：
文献类型：
--
作者：
Mohamad Ramlan Mohamed Salleh;N. Maruyama;M. Adachi;Naho Hontani;S. Saka;N. Kato;Y. Ohkawa;S. Utsumi
油菜种子含有十字花科植物素（11S球蛋白）、油菜籽蛋白（2S白蛋白）和油质蛋白（油体蛋白）作为主要种子蛋白。研究了压榨和干燥条件对菜籽粕中蛋白质提取的影响。实验条件对油体蛋白的提取影响很大，对十字花科蔬菜中十字在不同条件下，比较了十字花科植物中主要蛋白质十字花科植物素与大豆球蛋白（大豆11S球蛋白）的蛋白质理化性质。在一般情况下，十字花科植物蛋白表现出较高的表面疏水性，较低的热稳定性，以及较低和较高的溶解度，在mu= 0.5和mu = 0.08，分别比大豆球蛋白。在pH值（6.0，7.6，和9.0）和离子强度（mu= 0.08和0.5）检查，十字花科蔬菜的乳化能力比大豆球蛋白差，除了在mu= 0.08和pH值7.6。十字花科和大豆球蛋白的乳化能力与其热稳定性和表面疏水性无关。观察到较高的蛋白质浓度、较高的加热温度、较高的pH和较低的离子强度从十字花科植物素产生较硬的凝胶。凝胶硬度与十字花科植物素的结构稳定性部分相关。
Rapeseeds contain cruciferin (11S globulin), napin (2S albumin), and oleosin (oil body protein) as major seed proteins. The effects of oil expression and drying conditions on the extraction of these proteins from rapeseed meal were examined. The conditions strongly affected the extraction of oleosin and only weakly affected the extraction of cruciferin and napin. The protein chemical and physicochemical properties of cruciferin, the major protein present, were compared with those of glycinin (soybean 11S globulin) under various conditions. In general, cruciferin exhibited higher surface hydrophobicity, lower thermal stability, and lower and higher solubility at mu= 0.5 and mu = 0.08, respectively, than did glycinin. At the pHs (6.0, 7.6, and 9.0) and ionic strengths (mu= 0.08 and 0.5) examined, the emulsifying ability of cruciferin was worse than that of glycinin, except at mu= 0.08 and pH 7.6. The emulsifying abilities of cruciferin and glycinin did not correlate with thermal stability and surface hydrophobicity. Higher protein concentration, higher heating temperature, higher pH, and lower ionic strength were observed to produce harder gels from cruciferin. Gel hardness partly correlated with the structural stability of cruciferin.