Heteroprotein complex formation of bovine serum albumin and lysozyme: Structure and thermal stability
Heteroprotein complex formation of bovine serum albumin and lysozyme: Structure and thermal stability
复制标题
DOI：
10.1016/j.foodhyd.2017.08.016
复制
发表时间：
2018
影响因子：
10.7
通讯作者：
Monique Barreto Santos;C. W. P. D. Carvalho;E. Garcia-Rojas
中科院分区：
文献类型：
--
作者：
Monique Barreto Santos;C. W. P. D. Carvalho;E. Garcia-Rojas
采用浊度法和Zeta电位法研究了在不同蛋白质比例和NaCl浓度下，牛血清白蛋白（BSA）与溶菌酶（Lys）相互作用形成的杂蛋白复合物的pH变化。络合物在pH 8.0和11.0之间的范围内形成，其中在pH 9.0时的比率r = 0.5呈现最高络合。NaCl的加入降低了10 mM浓度下的相互作用。复合物的形成发生在蛋白质的等电点（pI）之间，接近电荷平衡，主要是通过静电相互作用，并有氢键的参与。差示扫描量热法表明，由于在67 °C形成单一变性点，相互作用产生了新的生物聚合物。形成的结构的平均尺寸为1.7 μm，远高于分离的蛋白质，显微镜分析显示复合物具有球形结构。BSA/Lys复合物可能是一种潜在的生物活性包封剂，并可用作食品配料。
The formation of a heteroprotein complex obtained by the interaction of bovine serum albumin (BSA) and lysozyme (Lys) was investigated by pH variation using turbidimetric analysis and zeta potential (ζ) at different protein ratios and NaCl concentrations. The complexes were formed in a pH range between 8.0 and 11.0, with the ratio r = 0.5 at pH 9.0 presenting the highest complexation. The addition of NaCl decreased the interaction at concentrations of 10 mM. The complex formation occurred between the isoelectric points (pI) of the proteins, close to a balance of charges, mainly by electrostatic interactions with some participation of hydrogen bonds. Differential scanning calorimetry suggested that the interaction gave rise to a new biopolymer due to the formation of a single denaturation point at 67 °C. The structures formed had an average size of ∼1.7 μm, well above that of the isolated proteins, and microscopic analysis revealed that the complexes had a globular structure. BSA/Lys complexes may be a potential bioactive encapsulating agent and may be used as a food ingredient.