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The effects of chemical modification of the amino groups of lysine residues on the activity of beta-1.3-glucanase from Spisula sachalinensis were studied. Modification of two lysine residues per molecule did not affect either the enzyme activity with respect to laminarine, nor the Km value. The modified beta-1.3-glucanase retains the ability to catalyze the transglycosylation and cleaves the high molecular weight CM-pachyman at the same rate as does the native enzyme. No significant changes in the enzyme thermal stability were observed. Thus, the modified enzyme groups cannot be involved in the enzyme active center and are exposed on the surface of the protein globule. The chemical modification was shown to have no effect on the enzyme kinetics, which is essential for its immobilization.
T G Svetasheva, and
V V Sova, and
L A Eliakova
February 2004,
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology,
T G Svetasheva, and
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L A Eliakova
December 2014,
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L A Eliakova
July 1970,
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T G Svetasheva, and
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L A Eliakova
March 1978,
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T G Svetasheva, and
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L A Eliakova
December 1982,
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T G Svetasheva, and
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L A Eliakova
June 1969,
Antonie van Leeuwenhoek,
T G Svetasheva, and
V V Sova, and
L A Eliakova
April 1988,
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T G Svetasheva, and
V V Sova, and
L A Eliakova
May 1983,
Biokhimiia (Moscow, Russia),
