Immobilization of -Fructofuranosidases from Aspergillus on Methacrylamide-Based Polymeric Beads for Production
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SRC="/images/gifchars/beta2.gif" BORDER=0 ALIGN="middle">-Fructofuranosidases from Aspergillus niger ATCC 20611and Aspergillus japonicusTIT-KJ1 were purified and immobilized covalently ontomethacrylamide-basedpolymeric beads. The porous, oxriane-containing support wasreactive and could bindenzymes in a buffered solution at room temperature with a density up to0.4 mg ofprotein g-1 of support with 100% immobilizedyield. Neither the optimum temperaturefor the highest enzymatic activities nor the batch reaction pattern forfructooligosaccharides formation catalyzed by s/gifchars/beta2.gif" BORDER=0 ALIGN="middle">-fructofuranosidases was changed byimmobilization.The amount of fructooligosaccharides produced from 50% (w/w)sucrose solution usingthe prepared immobilized enzymes was determined to be approximately60% of thetotal sugars in the reaction mixtures. This level offructooligosaccharides producedby the immobilized enzymes was comparable to that resulting fromprocessesemploying other immobilized biocatalysts as shown in the literature.The fraction oftotal fructooligosaccharides presented in the final mixture increasedwith the initialsucrose concentration, while fractions of glucose and fructosedecreased with anincrease sucrose concentration.

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