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20mM二硫苏糖醇(DTT)的存在时,用MTGase处理大约11h,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。
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.
出处
《现代食品科技》
EI
CAS
2010年第1期14-17,62,共5页
Modern Food Science and Technology
