Present study delineates the effects of sodium phosphate buffer (PBS) solutions on the stability of various proteins including lysozyme (Lys), bromelain (BM), hemoglobin (Hb), and human serum albumin (HSA). Different spectroscopic methods such as UV–visible, steady state fluorescence, temperature dependent fluorescence spectroscopy, Fourier transforms infrared spectroscopy (FTIR), circular dichroism (CD) spectroscopy and dynamic light scattering (DLS) show that PBS buffer protects protein structures. Efficacy of PBS stabilization from external additive factors follows order as lysozyme > BM > Hb. The thermal stability of HSA in PBS buffer solution was not detected, since no distinct and clear fluorescence transition was observed. However, results from other biophysical techniques reveal the native structure of HSA stabilized in presence of PBS. Moreover, increasing concentration of PBS also provides structural stabilization of HSA. This confirms the potentiality of PBS buffer as protecting agents for the proteins/enzymes. However, in case of Hb structure perturbed with the addition of higher concentrations of PBS. Our study confirms that efficacy of protein stabilization depends on type and concentration of buffer used. The present study is very useful for providing the alternative media to replace traditional volatile organic compounds or expensive modern solvents for biochemical applications.

目前的研究描述了磷酸钠缓冲液（PBS）溶液对各种蛋白质的稳定性的影响，包括溶菌酶（Lys），菠萝蛋白酶（BM），血红蛋白（Hb）和人血清白蛋白（HSA）。不同的光谱方法，例如紫外线可见光，稳态荧光，温度依赖性荧光光谱，傅立叶变换红外光谱（FTIR），圆二色性（CD）光谱和动态光散射（DLS）表明，PBS缓冲液可保护蛋白质结构。来自外部加性因子的PBS稳定作用的顺序为溶菌酶> BM> Hb。由于未观察到明显且清晰的荧光跃迁，因此未检测到HSA在PBS缓冲溶液中的热稳定性。然而，其他生物物理技术的结果揭示了在PBS存在下稳定的HSA天然结构。此外，增加的PBS浓度还可以提供HSA的结构稳定性。这证实了PBS缓冲液作为蛋白质/酶保护剂的潜力。但是，如果Hb结构受较高浓度PBS的扰动，则发生扰动。我们的研究证实，蛋白质稳定化的功效取决于所用缓冲液的类型和浓度。本研究对于为生化应用提供替代介质来代替传统的挥发性有机化合物或昂贵的现代溶剂非常有用。但是，如果Hb结构被较高浓度的PBS扰动，则发生扰动。我们的研究证实，蛋白质稳定化的功效取决于所用缓冲液的类型和浓度。本研究对于为生化应用提供替代介质来代替传统的挥发性有机化合物或昂贵的现代溶剂非常有用。但是，如果Hb结构受较高浓度PBS的扰动，则发生扰动。我们的研究证实，蛋白质稳定化的功效取决于所用缓冲液的类型和浓度。本研究对于为生化应用提供替代介质来代替传统的挥发性有机化合物或昂贵的现代溶剂非常有用。