Phenylalanine ammonia-lyase entrapped in fibers.
Phenylalanine ammonia-lyase extracted form Rhodotorula rubra (IFO 1101) was immobilized into cellulose triacetate fibers made hemocompatible by physical blend with a platelet anti-aggregating agent. The entrapped enzyme could operate at physiological values of phenylalanine and tyrosine reducing their level to traces within a few hours. The optimum pH value for the entrapped enzyme shifted from 8.0 to 9.0. At blood pH the activity was about 68 per cent of the maximum. The entrapped enzyme retained its original activity in blood for more than 50 days.
D000642:Ammonia-Lyases / Q000378:metabolism*; D002021:Buffers; D002482:Cellulose / Q000031:analogs & derivatives; D004800:Enzymes, Immobilized / Q000097:blood / Q000378:metabolism*; D066298:In Vitro Techniques; D010649:Phenylalanine / Q000378:metabolism; D010650:Phenylalanine Ammonia-Lyase / Q000097:blood / Q000378:metabolism*; D013696:Temperature; D014443:Tyrosine / Q000378:metabolism
D002021:Buffers; D004800:Enzymes, Immobilized; D014443:Tyrosine; D010649:Phenylalanine; D002482:Cellulose; C024671:cellulose triacetate; D000642:Ammonia-Lyases; D010650:Phenylalanine Ammonia-Lyase