title: [Xylose(glucose) isomerase reactivity of immobilized Arthrobacter sp].
abstract: The study of the xylose/glucose isomerase-containing Arthrobacter sp. B-5 cells immobilized in cobalt hydroxide gel showed that immobilization increases the substrate affinity of the enzyme, its thermo- and pH-optima of action and stability, and makes unnecessary the addition of stabilizing cobalt ions to the isomerization medium.
authors.affiliation: Institute of Microbiology, National Academy of Sciences of Belarus, ul. Kuprevicha 2, Minsk, 220141 Belarus. enzyme@mbio.bas-net.by
authors.forename: L I
authors.initials: LI
authors.lastname: Sapunova
authors.forename: A G
authors.initials: AG
authors.lastname: Lobanok
authors.forename: E V
authors.initials: EV
authors.lastname: Parakhnia
authors.forename: I O
authors.initials: IO
authors.lastname: Kazakevich
mesh_terms: D019747:Aldose-Ketose Isomerases / Q000737:chemistry / Q000378:metabolism*; D001173:Arthrobacter / Q000201:enzymology*; D003035:Cobalt; D005782:Gels; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D013379:Substrate Specificity; D013997:Time Factors
chemical_list: D005782:Gels; D003035:Cobalt; D019747:Aldose-Ketose Isomerases; C023298:xylose isomerase