Highly biocompatible enzyme aggregates crosslinked by L-lysine

Abstract

Aim: The purpose of the work is the use of L-Lysine amino acid cross-linker in the achievement of alternative and compatible enzyme aggregate. Cross-linked enzyme aggregates (CLEAs) were prepared from several enzymes ( glucose oxidase, peroxidase and urease) by precipitation and subsequent cross-linking using glutaraldehyde, 1,8-octanediamine and L-Lysine. Material and Methods: The effects of cross-linking agents on CLEAs activity were investigated and immobilized enzymes were characterized. The initial enzyme concentration was constant as 4x10(-3) mg/ml. BSA were used as precipitant in CLEA's method as described in our previously study. Results: The concentration of cross-linkers were 2% for glutaraldehyde and 1,8-octanediamine and 4% for L-Lysine. Activities of both free and immobilised enzymes were obtained by measuring the amount of substrate conversion, spectrophotometrically. Kinetic parameters of native and immobilised enzyme were calculated by using Lineweaver-Burk plots. Conclusion: L-Lysine was applied successfully as a cross-linker for the formation of CLEA's.