本文選題：β-乳球蛋白 + 蛋白纖維聚集體��； 參考：《湖北工業(yè)大學(xué)》2017年碩士論文

【摘要】：形狀各向異性顆粒具有獨(dú)特的界面活性,但可以應(yīng)用于食品中的形狀各向異性顆粒較少。β-乳球蛋白纖維聚集體是β-乳球蛋白(β-Lg)在特定條件下的自組裝產(chǎn)物。作為形狀各向異性顆粒的β-乳球蛋白纖維聚集體由于具有較好的界面活性,在食品工業(yè)中具有潛在的應(yīng)用價(jià)值。本文對(duì)β-乳球蛋白纖維聚集體的形成動(dòng)力學(xué)及其基本理化性質(zhì)進(jìn)行了表征,在此基礎(chǔ)上圍繞β-乳球蛋白纖維聚集體(fibrils)的界面、乳化特性及乳液消化行為做了系統(tǒng)研究。得出以下主要結(jié)論:1、β-乳球蛋白纖維可以在不存在任何其他表面活性劑的條件下形成穩(wěn)定的水包油型乳液。在遠(yuǎn)離等電點(diǎn)pI(pH=5.2)的條件下,β-乳球蛋白纖維能夠形成穩(wěn)定的水包油型乳液;而在pH 5.0時(shí),β-乳球蛋白纖維嚴(yán)重聚集并且形成的乳液不穩(wěn)定;當(dāng)β-乳球蛋白纖維濃度高于5 mg/mL時(shí)能形成穩(wěn)定的水包油乳液,且具有良好的長(zhǎng)期穩(wěn)定性,但乳液的粒徑較大。2、研究了β-乳球蛋白纖維在油-水界面的相互作用力。通過(guò)分析NaCl、Urea和Tween 80對(duì)纖維的界面吸附動(dòng)力學(xué)和流變行為的影響,發(fā)現(xiàn)在油-水界面上纖維聚集體之間以氫鍵相互作用和疏水相互作用為主,靜電相互作用為輔;同時(shí),NaCl、Urea和Tween 80的添加導(dǎo)致乳液的穩(wěn)定性降低,說(shuō)明氫鍵相互作用、疏水相互作用以及靜電相互作用是維持乳液穩(wěn)定性的重要因素。3、研究了β-乳球蛋白纖維乳液的模擬消化特性。通過(guò)比較β-乳球蛋白纖維聚集體、β-乳球蛋白和β-乳球蛋白球形納米顆粒穩(wěn)定的乳液的脂肪消化動(dòng)力學(xué),發(fā)現(xiàn)纖維聚集體穩(wěn)定的乳液消化速率最快,且脂肪酸釋放率最高,可達(dá)到70%;β-乳球蛋白納米顆粒穩(wěn)定的乳液脂肪消化速率最慢。其消化速率的不同是由三種不同乳化劑的界面性質(zhì)的差異所導(dǎo)致。
[Abstract]:The shape anisotropic particles have unique interfacial activity, but few of them can be used in food. 尾 -lactoglobulin fiber aggregates are self-assembled products of 尾 -lactoglobulin (尾 -Lg) under certain conditions. 尾-lactoglobulin fiber aggregates, as anisotropic particles, have potential application value in food industry due to their good interfacial activity. In this paper, the formation kinetics and physical and chemical properties of 尾 -lactoglobulin fiber aggregates were characterized, and the interface, emulsification characteristics and emulsion digestion behavior of 尾 -lactoglobulin fiber aggregates were systematically studied. The main conclusions are as follows: (1) 尾 -lactoglobulin fibers can form stable oil-in-water emulsion without any other surfactants. The 尾 -lactoglobulin fiber can form a stable oil-in-water emulsion at pH 5.2), while at pH 5.0, the 尾 -lactoglobulin fiber accumulates and the emulsion is unstable. When the concentration of 尾 -lactoglobulin fiber is higher than 5 mg/mL, a stable oil-in-water emulsion can be formed and has good long-term stability, but the particle size of the emulsion is larger. The interaction force of 尾 -lactoglobulin fiber at the oil-water interface is studied. By analyzing the effects of NaCl-Urea and Tween 80 on the interfacial adsorption kinetics and rheological behavior of the fibers, it is found that hydrogen bond interaction and hydrophobic interaction are dominant in the fiber aggregates at the oil-water interface, and the electrostatic interaction is the secondary one. At the same time, the addition of NaCl-Urea and Tween 80 reduced the stability of emulsion, which indicated that hydrogen bond interaction, hydrophobic interaction and electrostatic interaction were important factors to maintain the stability of emulsion. The simulated digestion characteristics of 尾 -lactoglobulin fiber emulsion were studied. By comparing the fat digestion kinetics of 尾 -lactoglobulin fiber aggregates, 尾 -lactoglobulin and 尾 -lactoglobulin spherical nanoparticles, it was found that the stable emulsion had the fastest digestion rate and the highest fatty acid release rate. The stability of 尾-lactoglobulin nanoparticles was the slowest rate of fat digestion in emulsion. The difference of digestion rate is caused by the interfacial properties of three different emulsifiers.
【學(xué)位授予單位】：湖北工業(yè)大學(xué)
【學(xué)位級(jí)別】：碩士
【學(xué)位授予年份】：2017
【分類(lèi)號(hào)】：TS201.2

【參考文獻(xiàn)】

相關(guān)博士學(xué)位論文 前2條

1 王金梅;大豆蛋白熱聚集行為及界面、乳化性質(zhì)研究[D];華南理工大學(xué);2012年

2 袁德保;大豆蛋白熱聚集行為及其機(jī)理研究[D];華南理工大學(xué);2010年

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本文編號(hào)：1895897