|
| 转谷氨酰胺酶途径的酶法糖基化修饰在蛋白质/多肽改性中的研究进展 |
| Progress on transglutaminase-catalyzed enzymatic glycosylation in protein/polypeptide modification |
| |
| DOI： |
| 中文关键词: 转谷氨酰胺酶 糖基化 糖肽 功能性质 |
| 英文关键词:transglutaminase glycosylation glycopeptide functional property |
| 基金项目: |
|
| Hits: 1061 |
| Download times: 613 |
| 中文摘要: |
| 为了拓展蛋白质的应用范围，常对蛋白质进行改性，其中转谷氨酰胺酶（TGase)催化的酶法糖基化反应已应用于多种蛋白质/多肽的改性中。为了对蛋白质/多肽的酶法糖基化技术的广泛应用提供参考，简述了TGase的来源、催化的反应类型和底物类型，重点阐述了糖基化蛋白/多肽糖基化程度的评价方法以及修饰产物功能性质的变化。目前，TGase主要来源于微生物，其可催化底物的交联、酰基转移（酶法糖基化）和脱酰基3种类型的反应。在TGase催化的酶法糖基化反应中，常用RP-HPLC、邻苯二甲醛（OPA）法和3，5-二硝基水杨酸（DNS）法评价糖基化程度。通过酶法糖基化反应，可以不同程度地改善底物的溶解性、乳化性、热稳定性等功能性质。TGase催化的酶法糖基化反应还存在反应体系复杂、糖基化效率低等问题，需要进一步研究解决。 |
| 英文摘要: |
| In order to expand the application scope of proteins, proteins are often modified, and the enzymatic glycosylation reaction catalyzed by transglutaminase (TGase) has been applied in the modification of various proteins/polypeptides. In order to provide a reference for the wide application of enzymatic glycosylation of protein/polypeptide, the source of TGase, types of reaction and substrate catalyzed by TGase were briefly described, and the evaluation methods of the glycosylation degree of glycosylated protein/polypeptide and changes of main functional properties of modified product were highlighted. At present, TGase is mainly derived from microorganisms, and it can catalyze three types of reaction, including substrate cross-linking, acyl transfer (enzymatic glycosylation) and deamidation. In TGase-catalyzed enzymatic glycosylation reactions, RP-HPLC, ortho-phthalaldehyde (OPA) and 3,5-dinitrosalicylic acid methods are commonly used to evaluate the degree of glycosylation. Functional properties of product such as solubility, emulsification, and thermal stability of substrates can be improved to varying degrees through enzymatic glycosylation. The enzymatic glycosylation reaction catalyzed by TGase still has problems such as complex reaction system and low glycosylation efficiency, and further research is needed to solve it. |
| 查看全文 View/Add Comment Download reader |
| Close |
|
|
|
