PMID: 2596845Dec 1, 1989

Preparation and properties of RNase T2 immobilized on concanavalin A-sepharose

Applied Biochemistry and Biotechnology
L G Reddy, V Shankar

Abstract

Partially purified RNase T2 (EC 2.7.7.17) from Aspergillus oryzae was bound through its carbohydrate moiety to Concanavalin A-Sepharose. The retention of activity was high, ranging from 70% at low enzyme load to approximately 9% at high enzyme load. Though there was no change in the pH and temperature optima, the pH stability and the Km decreased after immobilization. Compared to the soluble enzyme, the immobilized RNase T2 showed enhanced temperature stability and more resistance to metal ions. Both soluble and immobilized enzymes were stable to 8 M urea. On repeated use, the bound enzyme retained more than 60% of its initial activity after six cycles.

References

Dec 1, 1979·Archives of Biochemistry and Biophysics·H Y Hsiao, G P Royer
Aug 1, 1966·Journal of Biochemistry·T Uchida
Oct 9, 1964·Biochimica Et Biophysica Acta·A M MICHELSON

Citations

Apr 1, 1991·Enzyme and Microbial Technology·M Saleemuddin, Q Husain
Apr 1, 1994·Enzyme and Microbial Technology·M FisherB R Rabin
Jun 28, 2012·Nucleic Acids Research·Andrea ThornRalph Krätzner
Jan 1, 1993·Critical Reviews in Biotechnology·L G Reddy, V Shankar

Related Concepts

Bacillus intermedius secreted ribonuclease
concanavalin A-sepharose
Aspergillus oryzae
Endoribonucleases
Enzyme Stability
Hydrogen-Ion Concentration
Metals
Sepharose
Carmol

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