Chimie, Université de Montréal, 2900 Boulevard Edouard-Montpetit, Montréal, Québec, H3T 1J4, Canada.
Biomolecules. 2013 Oct 22;3(4):870-88. doi: 10.3390/biom3040870.
In nature, transglutaminases catalyze the formation of amide bonds between proteins to form insoluble protein aggregates. This specific function has long been exploited in the food and textile industries as a protein cross-linking agent to alter the texture of meat, wool, and leather. In recent years, biotechnological applications of transglutaminases have come to light in areas ranging from material sciences to medicine. There has also been a substantial effort to further investigate the fundamentals of transglutaminases, as many of their characteristics that remain poorly understood. Those studies also work towards the goal of developing transglutaminases as more efficient catalysts. Progress in this area includes structural information and novel chemical and biological assays. Here, we review recent achievements in this area in order to illustrate the versatility of transglutaminases.
在自然界中，转谷氨酰胺酶催化蛋白质之间形成酰胺键，从而形成不溶性蛋白质聚集体。这一特定功能长期以来一直被应用于食品和纺织工业，作为一种蛋白质交联剂，用于改变肉、羊毛和皮革的质地。近年来，转谷氨酰胺酶在从材料科学到医学等领域的生物技术应用中逐渐显现出来。人们也在努力深入研究转谷氨酰胺酶的基本原理，因为它们的许多特性仍未被充分了解。这些研究也致力于将转谷氨酰胺酶开发为更有效的催化剂。该领域的进展包括结构信息以及新的化学和生物学检测方法。在这里，我们综述了该领域的最新研究进展，以说明转谷氨酰胺酶的多功能性。
