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Prevention of limiting substrate diffusion in an immobilized enzyme reaction system lectin induced activation of gel entrapped beta d galactosidase



Prevention of limiting substrate diffusion in an immobilized enzyme reaction system lectin induced activation of gel entrapped beta d galactosidase



Biotechnology Letters 10(5): 301-306



Escherichia coli .beta.-D-galactosidase (EC 3.2.1.23) was entrapped in polyion complex-stabilized alginate gel beads together with a lectin from Ricinus communis (RCA1 lectin). The rate of entrapped enzyme-catalyzed hydrolysis of O-nitrophenyl-.beta.-D-galactoside dramatically increased with an increase in lectin content, and at the maximum level of lectin content the entrapped enzyme activity exceeded the native enzyme activity. A rapid decrease in the apparent Km was observed while increasing the lectin content, whereas the Vmax value varied insignificantly.

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