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Reversible immobilization of lysozyme via coupling to reversibly soluble polymer

Hen egg-white lysozyme (HEWL) can be covalently immobilized on a polymeric support (hydroxypropyl methylcellulose acetate succinate, AS-L), which is soluble above pH 5.5 but insoluble below pH 4.5. Commercial preparation of HEWL was used for the immobilization study. The immobilized enzyme (HEWL-AS)...

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Bibliographic Details
Published in:Enzyme and microbial technology 2003-10, Vol.33 (5), p.643-649
Main Authors: Chen, Sz-Hau, Yen, Yue-Horng, Wang, Chuan-Lu, Wang, San-Lang
Format: Article
Language:English
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Summary:Hen egg-white lysozyme (HEWL) can be covalently immobilized on a polymeric support (hydroxypropyl methylcellulose acetate succinate, AS-L), which is soluble above pH 5.5 but insoluble below pH 4.5. Commercial preparation of HEWL was used for the immobilization study. The immobilized enzyme (HEWL-AS) has much higher specific activity than those of free HEWL. The effects of pH and temperature on the activity and thermal stability of HEWL-AS were studied and compared with those of free HEWL. HEWL-AS retained nearly half of its initial chitinase activity even after heating at 70 °C for 50 min. The half-life at 4 °C was 4 days for free HEWL and 25 days for HEWL-AS. Following repeated pH cycles between 7 and 4.5, HEWL-AS retained nearly 50% of its original activity after 10 batches of chitinolytic reactions.
ISSN:0141-0229
1879-0909
DOI:10.1016/S0141-0229(03)00186-8