Enzyme stabilization via cross-linked enzyme aggregates.
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.
Gupta
Munishwar N
MN
Chemistry Department, Indian Institute of Technology Delhi, Hauz Khas, New Delhi, India. munishwar48@yahoo.co.uk
Raghava
Smita
S
D001709:Biotechnology / Q000379:methods*; D003432:Cross-Linking Reagents / Q000737:chemistry*; D004795:Enzyme Stability; D004798:Enzymes / Q000737:chemistry*; D004800:Enzymes, Immobilized / Q000276:immunology*; D005976:Glutaral; D006026:Glycoside Hydrolases; D008049:Lipase; D008855:Microscopy, Electron, Scanning; D010399:Penicillin Amidase; D013696:Temperature
D003432:Cross-Linking Reagents; D004798:Enzymes; D004800:Enzymes, Immobilized; D008049:Lipase; D006026:Glycoside Hydrolases; D010399:Penicillin Amidase; D005976:Glutaral