Enzyme Stabilization via Cross-Linked Enzyme Aggregates
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Extensive cross-linking of a precipitate of a protein by a cross-linking reagent (glutaraldehyde has been most commonly used) creates an insoluble enzyme preparation called cross-linked enzyme aggregates (CLEAs). CLEAs show high stability and performance in both conventional aqueous media as well as nonaqueous media. These are also stable at fairly high temperatures. CLEAs having more than one kind of enzyme activity can be prepared and such CLEAs are called combi-CLEAs or multipurpose CLEAs. Extent of cross-linking often influences their morphology, stability, activity, and enantioselectivity.
Key wordsCross-linking agents Glutaraldehyde Cross-linked enzyme aggregates Immobilization Thermal stability Enantioselectivity
This work was supported by funds obtained from Department of Science and Technology and Department of Biotechnology, both Government of India organizations. Finally, we thank our research group members (past and present); Dr. Kalyani Mondal, Dr. Shweta Shah, Abir Majumder, and Sohel Dalal, whose work has been described/quoted in this chapter.
Prof. Finn Wold, while at University of Minnesota, St. Paul, USA, introduced bifunctional reagents (more frequently called cross-linking reagents) to protein chemistry. Consequently several subsequent developments including CLEA design were possible. Prof. Wold was one of the early mentors of one of the authors (Munishwar N. Gupta). This chapter is dedicated to the memory of Prof. Finn Wold who was a great scientist and a great human being.
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