PEPTIDE-SYNTHESIS CATALYZED BY CROSS-LINKED ALPHA-CHYMOTRYPSIN IN WATER DIMETHYLFORMAMIDE SOLVENT SYSTEM

alpha-Chymotrypsin was crosslinked to give a water-insoluble polymer b y treatment with the bifunctional reagent glutaraldehyde, The specific activity of the crosslinked enzyme in aqueous media was three orders of magnitude lower than for the native chymotrypsin. In a medium conta ining more than 50% (v/v) of dimethylformamide the specific activities of both enzymes were comparable. In addition, the insoluble polymer w as more stable in the presence of 60% (v/v) dimethylformamide compared with the native enzyme. Therefore, in this medium enzymatic peptide s ynthesis could be successfully accomplished with the crosslinked enzym e, but not with the same amount of native chymotrypsin.