化工学报
化工學報
화공학보
JOURNAL OF CHEMICAL INDUSY AND ENGINEERING (CHINA)
2015年
6期
2196-2204
,共9页
刘洁%赵世玉%徐洲%常金明%陈意%范浩军
劉潔%趙世玉%徐洲%常金明%陳意%範浩軍
류길%조세옥%서주%상금명%진의%범호군
离子液体%胶原%溶解%再生%结构与性能变化
離子液體%膠原%溶解%再生%結構與性能變化
리자액체%효원%용해%재생%결구여성능변화
ionic liquids%collagen%dissolution%regeneration%changes of structure and properties
采用离子交换法,以1-丁基-3-甲基氯代咪唑([BMIM]Cl)为原料合成了咪唑醋酸盐型离子液体([BMIM]Ac),以两者为溶剂研究了胶原纤维在咪唑类离子液体中的溶解行为及再生前后的结构与热稳定性变化。结果表明,胶原纤维在CH3COO?和Cl?型离子液体中均能溶解,但具有明显不同的溶解特性。相对[BMIM]Cl的溶解性能而言,[BMIM]Ac能够在较低的温度下获得高浓度和良好流动性的胶原溶液,而且再生胶原的三股螺旋结构保留度更高。FTIR、UV、XRD、CD、TG 分析结果表明,胶原在咪唑离子液体中溶解前后其化学结构未发生明显变化,而三股螺旋的保留度和热稳定性略有降低。
採用離子交換法,以1-丁基-3-甲基氯代咪唑([BMIM]Cl)為原料閤成瞭咪唑醋痠鹽型離子液體([BMIM]Ac),以兩者為溶劑研究瞭膠原纖維在咪唑類離子液體中的溶解行為及再生前後的結構與熱穩定性變化。結果錶明,膠原纖維在CH3COO?和Cl?型離子液體中均能溶解,但具有明顯不同的溶解特性。相對[BMIM]Cl的溶解性能而言,[BMIM]Ac能夠在較低的溫度下穫得高濃度和良好流動性的膠原溶液,而且再生膠原的三股螺鏇結構保留度更高。FTIR、UV、XRD、CD、TG 分析結果錶明,膠原在咪唑離子液體中溶解前後其化學結構未髮生明顯變化,而三股螺鏇的保留度和熱穩定性略有降低。
채용리자교환법,이1-정기-3-갑기록대미서([BMIM]Cl)위원료합성료미서작산염형리자액체([BMIM]Ac),이량자위용제연구료효원섬유재미서류리자액체중적용해행위급재생전후적결구여열은정성변화。결과표명,효원섬유재CH3COO?화Cl?형리자액체중균능용해,단구유명현불동적용해특성。상대[BMIM]Cl적용해성능이언,[BMIM]Ac능구재교저적온도하획득고농도화량호류동성적효원용액,이차재생효원적삼고라선결구보류도경고。FTIR、UV、XRD、CD、TG 분석결과표명,효원재미서리자액체중용해전후기화학결구미발생명현변화,이삼고라선적보류도화열은정성략유강저。
1-butyl-3-methylimidazolium acetate ([BMIM]Ac) was synthesized from 1-butyl-3-methylimidazolium chloride ([BMIM]Cl) via the ion exchange method. These imidazolium ionic liquids (ILs) were used as solvents to dissolve collagen fibers. The solubility and the change of collagen structure as well as thermal stability after dissolution and regeneration from ILs were investigated. Athough collagen fibers could be dissolved in both CH3COO?and Cl?imidazolium ionic liquids, the dissolution characteristics were quite different. Compared with [BMIM]Cl ionic liquid, [BMIM]Ac was more advantageous to achieve a collagen solution with high concentration and good fluidity at a lower temperature, especially in retaining the integrity of collagen triple helix. FTIR, UV, XRD, CD and TG analysis were used to characterize the structure and properties of collagen before and after regeneration, and the results revealed that collagen chemical structure showed almost no change, but with slightly lower thermal stability and integrity of triple helix.