Effect of dextran and dextran modifications on the thermal and proteolytic stability of conjugated bovine testis beta-galactosidase and human serum albumin.
In order to study carbohydrate-induced protein stabilization bovine testis beta-galactosidase and human serum albumin were conjugated with dextran, partially acetylated dextran and partially methylated dextran. The conjugates and the free proteins were compared with respect to thermal stability at 50 degrees C and resistance to proteolytic digestion by subtilopeptidase A. Both beta-galactosidase and serum albumin were stabilized by conjugation with polysaccharide. However, higher stability was achieved by conjugating the proteins with the hydrophilic polysaccharides, dextran and acetylated dextran, than by conjugation with the hydrophobic polysaccharide, methylated dextran. The results are discussed in relation to possible explanations of carbohydrate-induced protein stabilization.
D000818:Animals; D002417:Cattle; D003911:Dextrans; D004355:Drug Stability; D004800:Enzymes, Immobilized / Q000378:metabolism; D005696:Galactosidases / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008297:Male; D012709:Serum Albumin / Q000378:metabolism*; D013381:Subtilisins; D013737:Testis / Q000201:enzymology*; D001616:beta-Galactosidase / Q000302:isolation & purification / Q000378:metabolism*
D003911:Dextrans; D004800:Enzymes, Immobilized; D012709:Serum Albumin; D005696:Galactosidases; D001616:beta-Galactosidase; D013381:Subtilisins