Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 348679
Title A Kinetic Model to Explain the Maximum in alpha-Amylase Activity Measurements in the Presence of Small Carbohydrates
Author(s) Baks, T.; Janssen, A.E.M.; Boom, R.M.
Source Biotechnology and Bioengineering 94 (2006)3. - ISSN 0006-3592 - p. 431 - 440.
DOI https://doi.org/10.1002/bit.20779
Department(s) Food Process Engineering
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2006
Keyword(s) enzymes - starch - assay
Abstract The effect of the presence of several small carbohydrates on the measurement of the -amylase activity was determined over a broad concentration range. At low carbohydrate concentrations, a distinct maximum in the -amylase activity versus concentration curves was observed in several cases. At higher concentrations, all carbohydrates show a decreasing -amylase activity at increasing carbohydrate concentrations. A general kinetic model has been developed that can be used to describe and explain these phenomena. This model is based on the formation of a carbohydrate-enzyme complex that remains active. It is assumed that this complex is formed when a carbohydrate binds to -amylase without blocking the catalytic site and its surrounding subsites. Furthermore, the kinetic model incorporates substrate inhibition and substrate competition. Depending on the carbohydrate type and concentration, the measured -amylase activity can be 75% lower than the actual -amylase activity. The model that has been developed can be used to correct for these effects in order to obtain the actual amount of active enzyme
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