Studying of properties of free and immobilized L-phenylalanine-ammonia-lyase from Rhodosporidium toruloides on silohrome С-80

L-phenylalanine-ammonia-lyase from Rhodosporidium toruloides immobilized with glutaraldehyde on silohrome С-80. Thermo- and pH-stability of free and immobilized preparation L-phenylalanine-ammonia-lyase, change of its activity at storage is studied. Dependence of activity of free and immobilized enzymatic preparation from a protein concentration in a reactionary mix and concentration of the buffer is investigated. The estimation of influence of concentration of L-phenylalanine on quantity of formed trans-cinnamon acid is spent. The rate of desamination of L-phenylalanine at increase in temperature of an incubation.