本项目通过生命科学领域中的大分子拥挤效应概念，利用分子排斥容积理论探讨大分子拥挤环境下蛋白分子构型趋于稳定并且与多糖进一步Maillard反应的本质关系。采用蛋白酶适度水解蛋白，打开蛋白分子的三级空间结构，使更多的肽链上ε-氨基基团与多糖的还原性羰基末端结合，揭示蛋白分子构型的变化与多糖生成蛋白多糖共价复合物（Protein- Polysaccharide Conjugate,PPC）的规律性认识；通过色谱及光谱技术研究蛋白分子构型变化及PPC结构、分析确定糖链与肽链连接的位点；重点研究蛋白分子构型的变化模式和程度，从分子形态学角度来探讨蛋白分子构型变化与大分子拥挤环境的内在关联，以期通过模拟设计大分子拥挤体系达到调控蛋白分子构型趋于稳定的科学问题。从而进一步揭示大分子拥挤环境下的蛋白质在反应过程中更少变性以及发生聚合/聚集，向着与多糖共价结合生成功能性大分子的反应方向进行的科学意义。

The project through macromolecular crowding effect of life science concepts, using molecular exclusion volume of macromolecular crowding environment discuss the relationship of protein molecular configuration tends to further stability and polysaccharide by Maillard reaction. Using protease moderately hydrolyzed protein, open the Three-dimensional structure of protein molecules, revealing the change of the structure of the protein molecule, so that the the more ε-amino group with the reducing end of the carbonyl group combined to generated Protein-Polysaccharide Conjugate (PPC); Study on the conformational changes of protein molecules and PPC structure through chromatographic and spectroscopic techniques, analysis to determine the sites connected by the polysaccharide chains with the polypeptide chain. Focus on protein molecular configuration changes mode and extent, from the perspective of molecular morphology to explore the inherent relationship of conformational changes of the protein molecules and macromolecular crowding environment. Through the analog design system to achieve regulatory protein molecular configuration tends to stabilize of the scientific problems. Further discloses fewer denatured proteins of the course of the reaction in macromolecular crowding environment and the occurrence of polymerization / aggregation, and toward covalent binding reaction with polysaccharide carried out in the direction of the generating conjugate. Macromolecular crowding environment is of great significance with special performance application of the reaction medium as the field of life sciences in the functional macromolecule.