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 430975
Title Enzyme inactivation kinetics: Coupled effects of temperature and moisture content
Author(s) Perdana, J.A.; Fox, M.B.; Schutyser, M.A.I.; Boom, R.M.
Source Food Chemistry 133 (2012)1. - ISSN 0308-8146 - p. 116 - 123.
DOI https://doi.org/10.1016/j.foodchem.2011.12.080
Department(s) Food Process Engineering
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2012
Keyword(s) heat inactivation - single-droplet
Abstract Enzymes are often dried for stability reasons and to facilitate handling. However, they are often susceptible to inactivation during drying. It is generally known that temperature and moisturecontent influence the enzymeinactivation kinetics. However, the coupledeffect of both variables on enzymeinactivation over a broad temperature–moisturecontent range is still not well understood. Therefore, the inactivation of ß-galactosidase in maltodextrin matrix is investigated using a newly developed method. An improved kinetic modelling approach is introduced, to predict the inactivation over a large range of temperature–moisture values. The model assumes a two-step inactivation mechanism involving reversible unfolding and irreversible inactivation. The model is able to describe the inactivation kinetics of ß-galactosidase accurately, showing the temperature-dependent kinetic transition from reversible unfolding to irreversible inactivation limited. Application of this approach can provide immediate understanding of the effect of processing on enzymeinactivation and indicates the processes’ critical points, which offers the possibility for optimisation.
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