Immobilized chymotrypsin on reversibly precipitable polymerized liposome.
A polymerized liposome (PLS) was prepared using a synthesized phosphatidylethanolamine with a diacetylene moiety that showed a reversibly precipitable property on addition and removal of salt. To prepare a soluble-insoluble immobilized enzyme, chymotrypsin was covalently immobilized on the outer surface of the PLS. The carbodiimide method was employed for the enzyme immobilization. Coupling was rapid and nearly complete at a weight ratio of enzyme to the PLS of < 0.12. The immobilized enzyme showed favorable activity yields for both low- and high-mol-wt substrates, i.e., 90 +/- 9% for N-benzoyl-L-tyrosine ethyl ester and 59 +/- 5% for casein up to an enzyme coupling density of 0.38 g/g-PLS. The immobilized enzyme was reusable and more stable at high temperature and long-term incubation than the native enzyme.[1]References
- Immobilized chymotrypsin on reversibly precipitable polymerized liposome. Sun, Y., Jin, X.H., Dong, X.Y., Yu, K., Zhou, X.Z. Appl. Biochem. Biotechnol. (1996) [Pubmed]
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