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- W1840028126 abstract "D-tagatose is produced from D-galactose by the enzyme L-arabinose isomerase (L-AI) in a commercially viable bioprocess. An active and stable biocatalyst was obtained by modifying chitosan gel structure through reaction with TNBS, D-fructose or DMF, among others. This led to a significant improvement in L-AI immobilization via multipoint covalent attachment approach. Synthetized derivatives were compared with commercial supports such as Eupergit(®) C250L and glyoxal-agarose. The best chitosan derivative for L-AI immobilization was achieved by reacting 4 % (w/v) D-fructose with 3 % (w/v) chitosan at 50 °C for 4 h. When compared to the free enzyme, the glutaraldehyde-activated chitosan biocatalyst showed an apparent activity of 88.4 U g (gel) (-1) with a 211-fold stabilization factor while the glyoxal-agarose biocatalyst gave an apparent activity of 161.8 U g (gel) (-1) with an 85-fold stabilization factor. Hence, chitosan derivatives were comparable to commercial resins, thus becoming a viable low-cost strategy to obtain high active L-AI insolubilized derivatives." @default.
- W1840028126 created "2016-06-24" @default.
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- W1840028126 date "2015-10-01" @default.
- W1840028126 modified "2023-10-16" @default.
- W1840028126 title "Chemical improvement of chitosan-modified beads for the immobilization of <i>Enterococcus faecium</i> DBFIQ E36 <scp>l</scp>-arabinose isomerase through multipoint covalent attachment approach" @default.
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- W1840028126 doi "https://doi.org/10.1007/s10295-015-1662-1" @default.
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