School of Food Science and Engineering, Yangzhou University, Jiangsu, Yangzhou 225127, China.
Food Chem. 2012 Dec 1;135(3):1245-52. doi: 10.1016/j.foodchem.2012.05.059. Epub 2012 May 19.
Lysozyme from hen egg white is a well-known antimicrobial protein with high ratio of hydrophobic and positively charged amino acid residues. In order to explore functional bioactivities of enzymatic hydrolysates of lysozyme, the protein was subjected to a simulated gastrointestinal digestion and the resulting hydrolysate (LPH2) showed a strong competitive angiotensin I-converting enzyme (ACE) inhibitory activity (IC(50)=12.6μg/ml) and a remarkable antioxidant activity. The LPH2 was fractionated using a 3kDa cut-off membrane and the obtained permeate LPH2-3kDa was analysed by MALDI-TOF-TOF MS. Using this technology, 38 different peptides were identified and some of these peptides were well fit with structure requirements of ACE inhibitory peptides and/or antioxidant peptides. The findings from this study suggest that the protein containing high proportion of hydrophobic and positively charged residues have the potential to generate multifunctional peptides, and these peptides would be beneficial ingredient to be used in functional foods.
来自鸡蛋清的溶菌酶是一种众所周知的具有高比例疏水性和正电荷氨基酸残基的抗菌蛋白。为了探索溶菌酶酶解产物的功能生物活性，将该蛋白进行了模拟胃肠道消化，得到的水解产物（LPH2）具有很强的竞争性血管紧张素 I 转换酶（ACE）抑制活性（IC50=12.6μg/ml）和显著的抗氧化活性。将 LPH2 用 3kDa 截止膜进行分级，然后用 MALDI-TOF-TOF MS 分析所得的透过液 LPH2-3kDa。使用该技术，鉴定出 38 种不同的肽，其中一些肽与 ACE 抑制肽和/或抗氧化肽的结构要求非常吻合。本研究表明，含有高比例疏水性和正电荷残基的蛋白质有可能产生多功能肽，这些肽将是功能性食品中有益的成分。
