[Preparation and properties of immobilized riboflavin kinase from Pichia guilliermondii].
Riboflavin kinase (ATP: riboflavin-5'-phosphotransferase, EC 2.7.1.26) from n-alkane utilizing Pichia guilliermondii yeast has been immobilized by covalent attachment to CNBr-activated agarose beads. The enzyme activity yield during immobilization reached 71.6%. Immobilized riboflavin kinase showed no significant changes in temperature and pH optima as well as in specificity of the action in relation to synthetic substrate analogues with the substitution of methyl groups at positions 7 and 8 of the isoalloxazine ring. Immobilized riboflavin kinase was stable during FMN synthesis in the continuous-flow packed column enzyme reactor with half-life of 27 days.
Kashchenko
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Preobrazhenskaia
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EN
Shavlovskiĭ
D004800:Enzymes, Immobilized / Q000032:analysis / Q000302:isolation & purification*; D010766:Phosphorylation; D010770:Phosphotransferases / Q000032:analysis / Q000302:isolation & purification*; D017853:Phosphotransferases (Alcohol Group Acceptor); D010843:Pichia / Q000201:enzymology*; D004718:Saccharomycetales / Q000201:enzymology*; D012995:Solubility; D013696:Temperature
D004800:Enzymes, Immobilized; D010770:Phosphotransferases; D017853:Phosphotransferases (Alcohol Group Acceptor); C022532:riboflavin kinase
Poluchenie i svoĭstva immovilizovannoĭ riboflavinkinazy iz drozhzheĭ Pichia guilliermondii.