【摘要】 本研究基于木瓜蛋白酶主要作用于赖氨酸和精氨酸等氨基酸、谷氨酰胺转氨酶催化蛋白质赖氨酸的ε-氨基和谷氨酸的γ-酰胺基结合的酶学特性，在利用木瓜蛋白酶催化苦杏仁蛋白限制性水解，使得更多赖氨酸残基暴露出来的基础上，利用谷氨酰胺转氨酶催化水解物的交联反应，从而改善苦杏仁蛋白的胶凝性，确定交联改性的最佳条件：谷氨酰胺转氨酶添加量16 U/g,交联温度38℃,pH值7.0,交联时间1.5 h,制得改性产物的胶凝性比改性前提高了209.43%,溶解性、持油性、乳化性也显著提高，起泡性、起泡稳定性略有提高，而持水性、乳化稳定性比改性前显著降低。改性产品的特性显著区别于天然苦杏仁蛋白，可为食品工业提供多样化的功能性蛋白。更多还原

【Abstract】 Based on the activity of papain acting mainly on the lysine and arginine residue and that of transglutaminase catalyzing protein cross-linking through the formation of interor intramolecular ε(γ-glutamyl) lysine isopeptidic bonds, papain was used for controlled hydrolysis of bitter almond kernel protein to increase the exposure of lysine residues, and subsequently transglutaminase was used to catalyze the crosslinking of the resulting bitter almond kernel protein hydrolysates, so as to enhance the gumminess of bitter almond kernel protein. The optimum conditions for the crosslinking reaction was established: transglutaminase dosage 16 U/g bitter almond kernel protein, temperature 38 ℃,pH 7.0,reaction time 1.5 h; And the modified bitter almond kernel protein thus prepared, in comparison to natural bitter almond kernel protein, it showed a gumminess 209.43% higher, along with significantly increased solubility, oil-holding and emulsifying capacity, slightly increased foaming capacity and foam stability, but it significantly reduced water-holding capacity and foam stability. The process optimized herein provides a protein with modified functional properties for diversified applications in the food industry.更多还原