Immobilization of single-strand specific nuclease (S1 nuclease) fromAspergillus oryzae |
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Authors: | L Gurucharan Reddy V Shankar |
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Institution: | (1) Division of Biochemical Sciences, National Chemical Laboratory, 411 008 Pune, India |
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Abstract: | S1 nuclease fromAspergillus oryzae (EC 3.1.30.1) was coupled to gelatin-alginate composite matrix using the residual free aldehyde groups on the surface of
glutaraldehyde crosslinked matrix. The immobilized enzyme retained approximately 10% activity of the soluble enzyme. When
partially purified enzyme was bound to the matrix, the immobilized preparation did not show any detectable enzyme activity.
However, the activity could be restored when the coupling was carried out in the presence of a coprotein or substrate. The
optimum pH of the immobilized S1 nuclease shifted to 3.8 from 4.3 for the soluble enzyme. Also, optimum temperature increased
to 65°C after immobilization. Bound S1 nuclease showed increased pH and temperature stabilities. Immobilization brought about
a twofold decrease in the Michaelis-Menton constant (K
m). |
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Keywords: | Single-strand specific nuclease fromAspergillus oryzae S1 nuclease immobilization S1 nuclease immobilization on crosslinked gelatin-alginate composite matrix immobilization in presence of a coprotein immobilization of nuclease |
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