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本文研究无花果蛋白酶（ＥＣ．３．４．４．１２）在不同浓度盐酸胍溶液中分子构象与活力变化关系。酶的内源荧光光谱，圆二色光谱与酶活力的变化表明：荧光光谱呈现二个明显的变化区域，低浓度胍（低于２ｍｏｌ／Ｌ）中，荧光发射峰基本不变，但荧光强度随胍浓度上升，随胍浓度断续增大（高于２ｍｏｌ／Ｌ），酶的最大发射波长明显红移。当胍浓度低于１ｍｏｌ／Ｌ时，不仅不会使酶失活，反而使酶激活，当胍浓度高于１ｍｏｌ／Ｌ以上时，酶逐渐失活，使酶完全失活的胍浓度为６ｍｏｌ／Ｌ酶的圆二色光谱也随着胍浓度的改变而发生复杂的变化。将荧光变化，ＣＤ谱变化及活力改变结合起来，表明活力的激活与构象的明显变化似是同步发生的，从另一角度进一步说明酶活性部位柔性是充分表现酶活力所必需。
This article studies the relationship between the molecular conformation and viability of fig protease (EC.3.4.4.12) in guanidine hydrochloride solution at different concentrations. The change of endogenous fluorescence, circular dichroism and enzyme activity showed that there were two obvious changes in the fluorescence spectrum. In low concentration guanidine (less than 2mol / L), the fluorescence emission peak remained basically unchanged, but the fluorescence intensity With guanidine concentration increased, with guanidine concentration intermittently increased (higher than 2mol / L), the maximum emission wavelength of the enzyme red-shift. When the concentration of guanidine is less than 1mol / L, not only will not inactivate the enzyme, but to activate the enzyme, when the guanidine concentration is higher than 1mol / L or more, the enzyme gradually inactivated, the enzyme completely inactivated guanidine concentration of 6mol / The circular dichroism of L-enzyme also undergoes complex changes with the concentration of guanidine. Fluorescence changes, changes in CD spectra and changes in vitality combined, indicating that the activation of vitality and conformation of the obvious changes seem to occur simultaneously, from another point of view that the activity of the enzyme site flexibility is fully necessary for the performance of enzyme activity.