Lipase-catalyzed synthesis and curing of high-molecular-weight polyricinoleate.
High-molecular-weight polyricinoleate, with an M(w) of 100,600, was enzymatically prepared by the polycondensation of methylricinoleate using immobilized lipase from Pseudomonas cepacia (IM-PC) in bulk in the presence of 4 A molecular sieves at 80 degrees C for 7 d. Polyricinoleate was a viscous liquid at room temperature with a glass transition temperature (T(g)) of -74.8 degrees C, showed no crystallinity and was biodegraded by activated sludge. Polyricinoleate was readily cured using a dicumyl peroxide at 170 degrees C for 30 min to produce a chloroform insoluble crosslinked polyricinoleate with a hardness of 50A using durometer A.
Ebata
Hiroki
H
Department of Applied Chemistry, Faculty of Science and Technology, Keio University, 3-14-1 Hiyoshi, Yokohama 223-8522, Japan.
Toshima
Kazunobu
K
Matsumura
Shuichi
S
D001593:Benzyl Compounds; D002384:Catalysis; D008049:Lipase / Q000737:chemistry*; D015394:Molecular Structure; D011108:Polymers / Q000138:chemical synthesis* / Q000737:chemistry; D012277:Ricinoleic Acids / Q000737:chemistry*; D013696:Temperature; D013997:Time Factors
D001593:Benzyl Compounds; D011108:Polymers; D012277:Ricinoleic Acids; D008049:Lipase; C037517:dicumyl peroxide