Borate buffer dramatically enhances the activity of poly(ethyleneglycol)-#alpha#-chymotrypsin complex catalytically active in anhydrous isooctane than conventional phosphate fubber even at low concentratoin

摘要

Poly(ethylene glycol)4000-#alpha#-chymotrysin (with a molar ratio of the polymer/enzyme of 8:1)complex prepared from borate buffe rsolutions had ca.6000- and 26-fold higher activity than native #alpha#-chymotrypsin and a complex prepared using a conventional phosphate buffer,respectively,enen at lower concentration (0.0474 mol g~(-1) enzyme) than that of norganic salts which were required for the enzyme activation.These results suggested that relatively hydrophobic buffers are desirable for preparing modifie denzymes that are catalytically active in organic media and contributed to develop more effective methodology for the optimal design of enzyme preparatios for nonaqueous enzymology.