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首页> 外文期刊>Biochimica et biophysica acta: BBA: International journal of biochemistry, biophysics and molecular biololgy. Proteins and Proteomics >Stability of the allergenic soybean Kunitz trypsin inhibitor
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Stability of the allergenic soybean Kunitz trypsin inhibitor

机译：变应性大豆Kunitz胰蛋白酶抑制剂的稳定性

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摘要

The soybean Kunitz trypsin inhibitor (SKTI) is a 21.5 kDa allergenic protein that belongs to the family of all antiparallel β-sheet proteins that are highly resistant to thermal and chemical denaturation. Spectroscopic and biochemical techniques such as circular dichroism (CD), ANS fluorescence and proteolysis were used to study its molecular structure under denaturing conditions such as acid and heat to which these allergens are commonly exposed during food processing. Reduction of native SKTI leads to its complete and rapid proteolysis by pepsin in simulated gastric fluid (SGF). Limited proteolysis with chymotrypsin during renaturation after heating showed that the native structure reforms at around 60 °C reversing the denaturation. CD spectra revealed that under acid denaturing conditions, SKTI shows major changes in conformation, indicating the possibility of a molten structure. The existence of this intermediate was established by ANS fluorescence studies at different concentrations of HCl. The remarkable stability of SKTI to both thermal and acid denaturation may be important for its role as a food allergen.
机译：大豆Kunitz胰蛋白酶抑制剂（SKTI）是一种21.5 kDa的变应原蛋白，属于所有对热和化学变性具有高度抵抗力的所有反平行β-sheet蛋白家族。光谱和生化技术（例如圆二色性（CD），ANS荧光和蛋白水解）用于研究在食品加工过程中这些变应原通常暴露于酸性和高温等变性条件下的分子结构。天然SKTI的减少导致其在胃酸模拟胃液（SGF）中被胃蛋白酶完全，快速地蛋白水解。加热后复性过程中用胰凝乳蛋白酶进行的有限的蛋白水解表明，天然结构在60°C左右发生重组，从而逆转了变性。 CD光谱表明，在酸变性条件下，SKTI显示出构象的主要变化，表明可能存在熔融结构。通过ANS荧光研究在不同的HCl浓度下确定了该中间体的存在。 SKTI对热和酸变性均具有显着的稳定性，可能对于其作为食物过敏原的作用很重要。

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