Enzymes in Organic Synthesis VII—Enzymatic Activity of Hrp After Chemical Modification of the Carbohydrate Moiety

Abstract

The carbohydrate moiety of horseradish peroxidase was conjugated with hexadecylamine or octylamine in a micellar medium. Recovery and purification of these conjugates was facilitated by the short length of the added spacers. The modification increased the liposolubility of the enzyme without detracting from its catalytic activity. For the hexadecylamine conjugate, the optimum reaction temperature was increased by 10°C. In addition, activity in organic solvents, such as toluene or chloroform, remained high, even at 70°C.

Immobilization of horseradish peroxidase on chitosan for use in nonaqueous media

“…1,2 The high synthetic potential of these biocatalysts has necessitated the development of various methodologies to delay both reversible and irreversible inactivation. Several strategies have been devised for enhancing the stability and activity of enzymes in organic media, such as chemical modification, 3 immobilization, 4,5 molecular imprinting with substrates, 6 the addition of effectors, 7 and the use of surfactants. 8,9 Substantial attention has been devoted to the covalent immobilization of enzymes to porous, insoluble supports such as glass, 10 alumina, 11 silica, 11 and chitosan [12][13][14][15][16][17][18][19][20][21] because they possess a high catalytic activity per unit volume of the catalyst and minimum diffusion limitations and facilitate the diffusion of large substrate molecules into the porous structure of the matrix within which enzymes are bound.…”