Effect of succinylation on the physicochemical properties of soy protein hydrolysate
Effect of succinylation on the physicochemical properties of soy protein hydrolysate
复制标题
DOI：
10.1016/s0963-9969(01)00063-1
复制
发表时间：
2001-01-01
影响因子：
8.1
通讯作者：
Zhang, W
中科院分区：
文献类型：
--
作者：
Achouri, A;Zhang, W
研究了大豆分离蛋白的酶解联合作用以及不同琥珀酸化程度对大豆蛋白水解物(SPH)理化性质的影响。结果表明，蛋白水解物经琥珀酸化后，得到主要的可溶性蛋白质组分，其相对分子质量为7 kDa。根据修饰程度的不同，琥珀酸化似乎既导致较高分子量组分(1000 kDa和400 kDa)的解离，也导致多肽由于分子间疏水相互作用而重新结合。由于施加较高的水解值，SPH的表面疏水性(S-0)显著降低。此外，净电荷和静电斥力的显著增加导致分子膨胀并经历构象变化，这反映在疏水性和荧光强度数据的变化上。总必需氨基酸含量在改性程度最高时略有下降。较低的琥珀酸化程度提高了大豆蛋白水解物的体外消化率，在69.5%琥珀酸化时达到最大值。(C)2001爱思唯尔科学有限公司。保留所有权利。
The combined effect of enzymatic hydrolysis of soy protein isolate and the influence of various levels of succinylation on the physicochemical properties of resulting soy protein hydrolysate (SPH) have been studied. The results indicated that proteolysis followed by succinylation resulted in a major soluble protein fraction having a molecular weight of 7 kDa. Depending on the level of modification, succinylation appeared to cause both dissociation of the higher molecular weight fractions (1000 and 400 kDa), and re-association of polypeptides as a result of intermolecular hydrophobic interactions. Surface hydrophobicity (S-0) of SPH decreased drastically due to the higher degree of hydrolysis value applied. Additionally, the significant increase in the net charge and elcectrostatic repulsion caused the molecules to expend and undergo conformational changes as reflected by the changes in the hydrophobicity and fluorescence intensity data. Total essential amino acid content was slightly lowered at the highest degree of modification. Low degrees of succinylation improved the in vitro digestibility of the soy protein hydrolysates, and the highest value was observed at 69.5% succinylation. (C) 2001 Elsevier Science Ltd. All rights reserved.