酶法疏水修饰大豆球蛋白对其色素结合能力的影响.pdfVIP

现代食品科技 Modern Food Science and Technology 2013, Vol.29, No.11 酶法疏水修饰大豆球蛋白对其色素结合能力的影响 杨晓泉，严江殷，侯俊杰 （华南理工大学轻工与食品学院，广东广州 510640） 摘要：为提高天然红曲色素的光稳定性，利用具有严格底物专一性的谷氨酰内肽酶对大豆球蛋白（11S）进行轻度水解,分析了 11S 酶解后表面疏水性的变化，并将水解产物与红曲色素形成蛋白/色素复合体，对两者之间的结合特性（结合常数、结合量）和复 合体的光稳定性进行了研究。研究发现，谷氨酰内肽酶对11S 的表面性质及红曲色素稳定性均具有显著影响。经谷氨酰内肽酶修饰后， 由于内部疏水基团的暴露，11S 的表面疏水性随水解度的增加而增加，与红曲色素的结合位点也随之变多。在中性条件下，水解度为 1.50%、质量分数为3%的11S 与红曲色素的结合常数达到最大值，最大结合量为215.00 U/g pro 。复合体经24 h 光照后，红曲色素的 色价保留率达90%，大大提高了红曲色素的光稳定性。 关键词：大豆球蛋白；色素；谷氨酰内肽酶；表面疏水性；结合 文章篇号：1673-9078(2013)11-2566-2570 Effect of Enzymatic Modification on Binding Capacity between Pigment and Glycinin YANG Xiao-quan, YAN Jiang-yin, HOU Jun-jie (College of Light Industry and Food Sciences , South China University of Technology, Guangzhou 510640, China) Abstract: To enhance photostability of Monascus pigment , glycinin was modified via glutamyl endopeptidase (GE), which had strict substrate specificity. The surface hydrophobicity of the 11S globulin after hydrolysis was analyzed, and protein/pigment complex was produced after enzymatic modification of the 11S. The binding propert ies (binding constant and binding capacity) and the light stability of protein/pigment complex were investigated. The results showed that GE had a significant effect on 11S surface character and Monascus pigment photostability. Surface hydrophobicity of 11S increases with the degree of hydrolysis (DH) increased after GE modifying as the inner hydrophobic groups exposed. At pH 7.0, the binding constants of Monascus pigment and 3% (m/V) 11 S reached the maximum of 215.00 U/g pro when the DH was 1.50%. After 24 h light exposure, the protein/pigment complex had the color value retention rate of 90% which highly improved the li