title: Preparation and properties of RNase T1 immobilized on aminoethyl Bio-Gel P-2.
abstract: The partially purified RNase T1, when coupled to glutaraldehyde activated aminoethyl Bio-Gel P-2, retained 22-24% activity of the soluble enzyme. Immobilization resulted in an increase in the optimum temperature and temperature stability, but it did not affect the pH optimum. Km and Vmax decreased as a result of immobilization. The bound enzyme showed high stability to repeated use and storage.
authors.affiliation: Division of Biochemical Sciences, National Chemical Laboratory, Pune, India.
authors.forename: S
authors.initials: S
authors.lastname: Gite
authors.forename: V
authors.initials: V
authors.lastname: Shankar
mesh_terms: D001236:Aspergillus oryzae / Q000201:enzymology; D004795:Enzyme Stability; D004800:Enzymes, Immobilized; D005782:Gels; D005976:Glutaral / Q000378:metabolism; D007700:Kinetics; D006163:Ribonuclease T1 / Q000302:isolation & purification / Q000378:metabolism*; D012995:Solubility; D013696:Temperature
chemical_list: D004800:Enzymes, Immobilized; D005782:Gels; D006163:Ribonuclease T1; D005976:Glutaral