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首页> 外文OA文献 >Functionality of whey proteins covalently modified by allyl isothiocyanate. Part 1 physicochemical and antibacterial properties of native and modified whey proteins at pH 2 to 7
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Functionality of whey proteins covalently modified by allyl isothiocyanate. Part 1 physicochemical and antibacterial properties of native and modified whey proteins at pH 2 to 7

机译：异硫氰酸烯丙酯共价修饰的乳清蛋白的功能。第1部分在pH 2至7的天然和修饰乳清蛋白的理化和抗菌特性

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摘要

Whey protein isolate (WPI) (∼75% β-lactoglobulin (β-LG)) is frequently used in foods as a natural emulsifying agent. However, at an acidic pH value, its emulsification capacity is greatly reduced. The covalent attachment of natural electrophilic hydrophobic molecules to WPI proteins is a promising method for changing the physicochemical properties of WPI in favor of a higher functionality at acidic pH values.In the present study, different concentrations of allyl isothiocyanate (AITC) were covalently bound to WPI and the related changes in physicochemical properties (charge, aggregation, surface hydrophobicity and secondary structure) were monitored over a wide pH range (pH 2 to 7). In addition, the antibacterial activity against different strains of S. aureus and E. coli before and after AITC modification was assessed.The results showed that both whey proteins β-LG and α-lactalbumin (ALA) were modified by AITC. This modification remained stable during pH adjustment. Unbound AITC was successfully removed by the lyophilization process, which reduced the strong odor of the volatile AITC. A shift of the isoelectric point towards acidic conditions was observed. The hydrophobicity of the modified WPI increased significantly and the protein's secondary and tertiary structure was altered. In addition, a more loose protein folding was observed. These effects were less pronounced at pH 6 and 7. The relatively mild antibacterial effect of native WPI was not significantly influenced by the addition of AITC.
机译：乳清蛋白分离物（WPI）（〜75％β-乳球蛋白（β-LG））经常在食品中用作天然乳化剂。但是，在酸性pH值下，其乳化能力大大降低。天然亲电子疏水性分子与WPI蛋白的共价结合是改变WPI的理化性质以在酸性pH值上具有更高功能的一种有前途的方法。在本研究中，不同浓度的异硫氰酸烯丙酯（AITC）共价结合在较宽的pH范围（pH 2至7）中监测WPI和理化性质（电荷，聚集，表面疏水性和二级结构）的相关变化。此外，还评估了AITC修饰前后金黄色葡萄球菌和大肠杆菌对不同菌株的抗菌活性，结果表明AITC修饰了乳清蛋白β-LG和α-乳白蛋白（ALA）。在pH调节过程中，这种修饰保持稳定。冻干过程成功去除了未结合的AITC，从而减少了挥发性AITC的强烈气味。观察到等电点向酸性条件的移动。修饰的WPI的疏水性显着增加，并且蛋白质的二级和三级结构发生了变化。另外，观察到更宽松的蛋白质折叠。在pH为6和7时，这些作用不太明显。加入AITC不会明显影响天然WPI的相对温和的抗菌作用。

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