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  • Title: Mannan-penicillin G acylase neoglycoproteins and their potential applications in biotechnology.
    Author: Masárová J, Mislovicová D, Mendichi R, Svitel J, Gemeiner P, Danielsson B.
    Journal: Biotechnol Appl Biochem; 2004 Jun; 39(Pt 3):285-91. PubMed ID: 15154839.
    Abstract:
    Mannan-penicillin G acylase neoglycoproteins were prepared by the conjugation of Saccharomyces cerevisiae mannan with enzyme penicillin G acylase using the reductive amination method. Eight neoglycoproteins preparations were obtained after gel chromatography. The preparations contained from 42 to 67% (w/w) saccharides and their molar masses varied from 283 to over 1000 kDa. Significant biospecific interaction of separated fractions with the lectin concanavalin A was evaluated by the precipitation and sorption method (equilibrium constants) and further characterized using surface plasmon resonance to determine kinetic association and dissociation constants. K (D) was determined over the range 10(-7) M. High-molar-mass preparations appeared to be more suitable for preparation of stable and active complexes with concanavalin A for prospective use as a penicillin G acylase biocatalyst in enzyme reactors. The enzyme stability of such complexes was significantly increased compared with the original neoglycoprotein. Lower-molar-mass preparations were more suitable for applications such as biocatalysts in bioanalytical devices.
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