Coaggregate of trypsin and chymotrypsin

Abstract

The method of chemical aggregation of enzymes has the advantage of yielding an immobilized enzyme preparation wherein reactor volume can be significantly reduced because of the absence of an inert carrier. A coaggregate of trypsin and chymotrypsin formed by extensive cross-linking with glutaraldehyde is described. A significant property of this aggregate is the reduced autolysis of the trypsin component of the coaggregate.

Immobilization of Biological Catalysts

“…The mechanism of the crosslinking reaction is not fully understood to date, which might partly be due to the diverse mono-and polymeric forms of glutaraldehyde in commercially available preparations. While covalent crosslinking of whole-cell biocatalysts usually starts from cell suspensions mixed with spacer molecules such as polyethyleneimine [37], gelatin, or albumin [38][39][40], solutions [30,41,42] as well as spray-dried [43], crystalline [44,45], or pre-aggregated preparations [46] can be used for the crosslinking of isolated enzymes. [28]).…”