酪蛋白巨肽对乳球蛋白热变性热聚合的影响研究-食品科学专业论文.docxVIP

哈尔滨工业大学工学硕士学位论文 哈尔滨工业大学工学硕士学位论文 目录 目录 PAGE PAGE IV III III Abstract Whey protein is widely adopted in food industry due to its superior physiochemical features including interfacial characteristics and gelatination. Caseino-macropeptide (CMP) is a hydrolysate of k-casein, and is existing in most whey powders. Due to different production methods, commercial whey protein concentrated (WPC) and whey proteinisolated (WPI) are different in CMP. The physiochemical properties of CMP may change the functions of whey proteins when used as ingredient, which may limit its use in some productions. In this paper, the heat denaturation dynamics affluence by CMP to β-lactoglobulin under different heat treatment temperatures is studied; the size and structure of CMP-β Lg polymerization products under different heat denaturation circumstances are compared; the reaction mechanism of heat denaturation and heat aggregation of CMP/β-Lg is also discussed. In this paper, the natural β-Lg residue in heating process is analyzed by HPLC, and the dynamic influence of heat denaturation/aggregation from CMP to β-Lg is discussed in four aspects: pH, mass proportion, heating temperature and strength of calcium-ion. The result shows, pH and CMP mass proportion are able to influence the speed of heat denaturation process (P0.05). When pH=6.7, Ca2+ could markedly accelerate the heat denaturation and CMP could lessen its significance. However; when pH=4.0, Ca2+ is insignificant in the acceleration of β-Lg heat denaturation process, but it will lessen the significance of the influence of CMP. Besides that, scattered spectrum method is adopted for analyzing the molecule radius of the resulting aggregates, and non-degenerate gelatin electrophoresis is adopted to analyze the aggregation degree of the resulting aggregate. The result shows, the reaction mechanism of heat denaturation/aggregation and the affection mechanism of CMP to the reaction are different when pH=6.7 and 4.0. When pH=6.7, the main