本文選題：抗凍蛋白 + 熱滯活性�。� 參考：《內(nèi)蒙古大學(xué)》2016年碩士論文

【摘要】：抗凍蛋白(antifreeze proteins, AFPs)是一類(lèi)結(jié)構(gòu)多樣且具有特殊功能的蛋白質(zhì)。它能夠以非依數(shù)性的方式使溶液的冰晶生長(zhǎng)點(diǎn)降低,但不影響其熔點(diǎn),從而使冰晶生長(zhǎng)點(diǎn)和熔點(diǎn)之間出現(xiàn)了差值,即為熱滯值(Thermal Hysteresis, TH)。因?yàn)榭箖龅鞍姿哂械奶厥饪箖鲂?yīng),使其存在巨大的商業(yè)價(jià)值,并且在生物工程、制藥、醫(yī)學(xué)、食品等方面都有廣闊的應(yīng)用前景。最新實(shí)驗(yàn)研究表明,抗凍蛋白在冰晶表面的吸附是一個(gè)隨著時(shí)間不斷積累的不可逆過(guò)程,并且退火溫度不同時(shí),所得到的熱滯活性不同,熱滯活性會(huì)隨著退火溫度的降低而增大。當(dāng)退火溫度以一定的速率下降時(shí),抗凍蛋白的熱滯活性會(huì)隨著降溫速率的增大而減小。以上實(shí)驗(yàn)結(jié)果表明,抗凍蛋白的熱滯活性除了與抗凍蛋白溶液的濃度有關(guān)之外,還與抗凍蛋白在冰晶表面吸附結(jié)合的時(shí)間、退火溫度以及降溫速率等因素有關(guān)。本文基于吸附一抑制理論,根據(jù)抗凍蛋白在冰晶表面的吸附動(dòng)力學(xué)過(guò)程,建立了抗凍蛋白吸附的二維不可逆動(dòng)力學(xué)模型,并且首次在低過(guò)冷度條件下討論第三類(lèi)魚(yú)抗凍蛋白的熱滯活性的問(wèn)題中考慮了溶液中的水分子對(duì)其吸附的影響。認(rèn)為在一定過(guò)冷溫度范圍內(nèi),水分子會(huì)因增加冰晶表面的結(jié)合位點(diǎn)而對(duì)抗凍蛋白的吸附有一定促進(jìn)作用。但是溫度過(guò)低時(shí),水分子將會(huì)占據(jù)絕對(duì)優(yōu)勢(shì)而使冰晶不可控制地快速生長(zhǎng)。文中根據(jù)實(shí)驗(yàn)數(shù)據(jù)擬合得到了退火溫度保持在低于熔點(diǎn)下一定數(shù)值恒定不變、以及以一定速率下降時(shí)水分子和第三類(lèi)魚(yú)抗凍蛋白之間的競(jìng)爭(zhēng)關(guān)系,根據(jù)抗凍蛋白分子結(jié)合在冰晶表面所引起表面空位點(diǎn)分布的變化,計(jì)算出冰晶表面的覆蓋度隨時(shí)間的變化,進(jìn)而得出熱滯活性隨時(shí)間變化的關(guān)系,并將計(jì)算結(jié)果與實(shí)驗(yàn)數(shù)據(jù)進(jìn)行了對(duì)比,結(jié)果符合較好。
[Abstract]:Antifreeze proteins (AFPs) are a class of proteins with various structures and special functions. It can decrease the growth point of ice crystal without affecting the melting point of the solution in a non-numerical manner, thus the difference between the growth point of ice crystal and the melting point appears, that is, the thermal hysteresis value is thermal hysterics, THN. Because of its special antifreeze effect, antifreeze protein has great commercial value, and has broad application prospects in biological engineering, pharmacy, medicine, food and so on. The latest experimental studies show that the adsorption of antifreeze proteins on the surface of ice crystals is an irreversible process accumulated over time, and the thermal hysteresis activity is different at different annealing temperatures. The thermal hysteresis activity increases with the decrease of annealing temperature. When the annealing temperature decreases at a certain rate, the thermal hysteresis activity of the antifreeze protein decreases with the increase of the cooling rate. The results show that the thermal hysteresis activity of antifreeze proteins is not only related to the concentration of antifreeze protein solution, but also related to the time of adsorption and binding of antifreeze proteins on the ice crystal surface, annealing temperature and cooling rate and so on. Based on the adsorption-inhibition theory, a two-dimensional irreversible kinetic model of antifreeze protein adsorption was established according to the adsorption kinetics of antifreeze protein on the ice crystal surface. The effect of water molecules in solution on the adsorption of the third kind of fish antifreeze proteins was considered for the first time in the study of the thermal hysteresis activity of the third kind of fish antifreeze proteins under the condition of low undercooling. It is concluded that water molecules can promote the adsorption of antifreeze proteins by increasing the binding sites on the ice crystal surface within a certain range of undercooling temperature. But when the temperature is too low, water molecules will dominate and make ice crystals grow uncontrollably fast. According to the experimental data, the competitive relationship between the water molecules and the third kind of fish antifreeze proteins is obtained when the annealing temperature is kept below the melting point and the value is constant, and when the temperature drops at a certain rate. According to the change of the surface vacancy distribution caused by the binding of antifreeze protein molecules on the ice crystal surface, the variation of the surface coverage with time is calculated, and the relationship between the thermal hysteresis activity and the time is obtained. The calculated results are compared with the experimental data and the results are in good agreement.
【學(xué)位授予單位】：內(nèi)蒙古大學(xué)
【學(xué)位級(jí)別】：碩士
【學(xué)位授予年份】：2016
【分類(lèi)號(hào)】：O647.3;O629.73

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