Glucoamylase covalently coupled to porous glass |
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Authors: | Li Gaoxiang Huang Jiayu Kou Xiufen Zhang Shuzheng |
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Institution: | (1) Institute of Microbiology, Academia Sinica, Beijing, China |
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Abstract: | Glucoamylase (EC 3.2.1.3) was immobilized to alkylamine porous glass with glutaraldehyde. The choice and pretreatment of carrier
and conditions for immobilization have been investigated. The immobilized enzyme contained about 4.0–8.0% protein and its
activity was about 1000–1700 U/g. Some characteristics of the immobilized enzyme and the native enzyme have been comparatively
investigated. The optimum temperature and the pH stability of the preparation were almost identical to the native one. However,
the optimum pH of bound glucoamylase shifted 1.3 pH units toward the alkaline side compared to the native one. The Michaelis
constant(K
m
) of bound glucoamylase for soluble starch was about four times higher than that of the native enzyme, whileK
m
values for maltose approached those of the native material. At 45‡C the half-life of IMG was 104 days under operational conditions.
Alkaline protease, α-amylase, asparaginase, and penicillin acylase were also chemically coupled to porous glass by the same
method and high relative activities were obtained. |
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Keywords: | Glucoamylase coupling to porous glass covalent coupling of glucoamylase to porous glass glass coupling of glucoamylase to porous |
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