2000Journal of Chemical Technology & BiotechnologyRequires access

A kinetic model for enzymatic wheat starch saccharification

Christina �kerberg, Guido Zacchi, Nelson Torto, Lo Gorton

Open publisher page 39 citations

Abstract

A kinetic model describing the enzymatic saccharification of wheat starch by a mixture of α-amylase and amyloglucosidase has been developed. The model describes the influence of pH, glucose inhibition and starch and enzyme concentration. The results of experimental saccharification under different physical conditions, eg pH and temperature, were used to determine the parameters in the model. The dominant enzyme in the mixture was amyloglucosidase and the maximum rate of saccharification due to this enzyme was found to be optimal at pH 5, and increased Five-Fold when the temperature was increased from 30 to 55 °C. Saccharification due to the action of amyloglucosidase was inhibited by the glucose produced and simulation showed that the maximum rate of saccharification decreased by 58% at a starch concentration of 140 g dm−3 compared with a starch concentration much less than 110 g dm−3 where the effect of glucose inhibition was negligible. © 2000 Society of Chemical Industry

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What this paper is about

A kinetic model describing the enzymatic saccharification of wheat starch by a mixture of α-amylase and amyloglucosidase has been developed. The model describes the influence of pH, glucose inhibition and starch and enzyme concentration. The results of experimental saccharification under different physical conditions, eg pH and temperature, were used to determine the parameters in the model. The dominant enzyme in the mixture was amyloglucosidase and the maximum rate of saccharification due to this enzyme was found to be optimal at pH 5, and increased Five-Fold when the temperature was increased from 30 to 55 °C. Saccharification due to the action of amyloglucosidase was inhibited by the glucose produced and simulation showed that the maximum rate of saccharification decreased by 58% at a starch concentration of 140 g dm−3 compared with a starch concentration much less than 110 g dm−3 where the effect of glucose inhibition was negligible. © 2000 Society of Chemical Industry

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Available abstract

A kinetic model describing the enzymatic saccharification of wheat starch by a mixture of α-amylase and amyloglucosidase has been developed. The model describes the influence of pH, glucose inhibition and starch and enzyme concentration. The results of experimental saccharification under different physical conditions, eg pH and temperature, were used to determine the parameters in the model. The dominant enzyme in the mixture was amyloglucosidase and the maximum rate of saccharification due to this enzyme was found to be optimal at pH 5, and increased Five-Fold when the temperature was increased from 30 to 55 °C. Saccharification due to the action of amyloglucosidase was inhibited by the glucose produced and simulation showed that the maximum rate of saccharification decreased by 58% at a starch concentration of 140 g dm−3 compared with a starch concentration much less than 110 g dm−3 where the effect of glucose inhibition was negligible. © 2000 Society of Chemical Industry

Key concepts: Hydrolysis, Chemistry, Starch, Amylase, Enzyme, Enzymatic hydrolysis, Food science, Chromatography

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