采用激光光散射技术研究转谷氨酰胺酶催化的β-乳球蛋白交联反应 A Laser Light Scattering Study of Transglutaminase-induced Cross-linking Reaction.pdfVIP

现代食品科技 Modern Food Science and Technology 2010, Vol.26, No.1 采用激光光散射技术研究转谷氨酰胺酶催化的β-乳 球蛋白交联反应 刘付，王昌盛，唐传核 （华南理工大学 轻工与食品学院，广东广州 510640） 摘要：采用体积排阻色谱(SEC)联合多角度激光光散射法(MALLS)技术研究了由微生物转谷氨酰胺酶(MTGase)诱导的 β-乳球蛋 白的体外交联反应。结果表明，在20 mM 二硫苏糖醇（DTT ）的存在时，用MTGase 处理大约 11 h，会逐渐形成高分子量的高聚物 或寡聚体，同时 β-乳球蛋白会由二聚体向单体转变。在 DTT 不存在时，同样有这种转变。上述结果表明，MTGase 处理可作为一种 很有潜力的技术，可于调控许多球蛋白的热稳定性。 关键词：β-乳球蛋白；微生物转谷氨酰胺酶(MTGase)；交联；激光光散射 文章编号：1673-9078(2010)1-14-5 A Laser Light Scattering Study of Transglutaminase-induced Cross-linking Reaction LIU Fu, WANG Chang-sheng, Tang Chuan-He (South China University of Technology, College of Light Industry and Food Sciences, 510640 Guangzhou) Abstract: The in situ cross-linking reaction of β-lactoglobulin (β-LG) induced by microbial transglutaminase (MTGase) was investigated using size-exclusion chromatography (SEC) combined with multi-angle laser light scattering (MALLS). The results indicated that, in the presence of 20 mM dithiothreitol (DTT), the MTGase treatment up to about 11 h gradually resulted in the formation of biopolymers or oligomers with higher molecular weight (MW), and the transformation of dimeric form of β-LG to its monomeric form. This transformation was also observed in the absence of DTT. These data suggested that MTGase treatment could be utilized as a potential technique to modulate the thermal stability of many globular proteins. Key words: β-Lactoglobulin; Microbial translgutaminase (MTGase); Cross-linking; Laser light scattering [6,7] [8-9] 酶促交联或聚合反应被证明能够改善食品蛋白质 DTT ） 或酶处理前进行热处理 。 的一些功能性质，包括水化性质、热性质和其他与表 热稳定性是乳清蛋白（特别是β-