摘要
研究了利用马来酸酐对胶原蛋白进行改性,使胶原蛋白能在有机溶剂中溶解并提高其与异氰酸酯之间的反应速率,研究了改性反应对胶原蛋白与异氰酸酯之间反应的影响。结果表明:胶原蛋白经过改性后在DMF溶剂中的溶解度大于50%,与甲苯二异氰酸酯之间的反应时间由改性前的48h缩短为60min,为聚氨酯改性胶原蛋白的制备提供了条件。
Collagen protein was modified by maleic anhydride to improve its solubility in organic solvent and to increase the reaction rate between isocyanate and collagen protein. The factors that affect the modifying reaction of collagen and the interaction between isocyanate and collagen were studied. The experimental results show that after the modification the solubility of collagen protein in DMF is beyond 50% and the time for reaction of toluene diisocyanate and collagen is reduced from 48 hours to 60 minutes, which are helpful for the preparation of polyurethane - modified collagen protein.
出处
《中国皮革》
CAS
北大核心
2010年第3期18-22,共5页
China Leather
基金
国家自然科学基金项目(20676144)
关键词
胶原蛋白
马来酸酐
异氰酸酯
改性
机理
collagen
maleic anhydride
isocyanate
modification
mechanism