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Thermal stability of invertase in reduced-moisture amorphous matrices in relation to glassy state and trehalose crystallization
The thermal stability of enzyme invertase in reduced-moisture model systems of maltodextrin (MD), polyvynilpyrrolidone (PVP; MW 40,000) and trehalose heated at 90 degrees C was studied. Significant invertase inactivation was observed in heated glassy PVP and MD systems kept well below their glass tr...
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Published in: | Journal of food science 1997-01, Vol.62 (1), p.105-112 |
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container_title | Journal of food science |
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creator | Cardona, S. (Univ. de Buenos Aires, Buenos Aires, Argentina.) Schebor, C Buera, M.P Karel, M Chirife, J |
description | The thermal stability of enzyme invertase in reduced-moisture model systems of maltodextrin (MD), polyvynilpyrrolidone (PVP; MW 40,000) and trehalose heated at 90 degrees C was studied. Significant invertase inactivation was observed in heated glassy PVP and MD systems kept well below their glass transition temperature (T(g)), but the enzyme was fairly stable in rubbery trehalose systems. However, at moisture contents which allowed trehalose crystallization rapid thermal inactivation of invertase was observed. Invertase inactivation in heated PVP, MD and trehalose systems of reduced-moisture could not be predicted on the basis of glass transition and this was particularly true for trehalose. Conditions which would allow collapse of the systems and crystallization of trehalose were fairly well predicted based on the estimated T(g) of model systems |
doi_str_mv | 10.1111/j.1365-2621.1997.tb04378.x |
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Invertase inactivation in heated PVP, MD and trehalose systems of reduced-moisture could not be predicted on the basis of glass transition and this was particularly true for trehalose. Conditions which would allow collapse of the systems and crystallization of trehalose were fairly well predicted based on the estimated T(g) of model systems</description><subject>Biological and medical sciences</subject><subject>CRYSTALLIZATION</subject><subject>Enzymes</subject><subject>Food engineering</subject><subject>Food industries</subject><subject>Food science</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General aspects</subject><subject>GLASS TRANSITION</subject><subject>HEAT</subject><subject>HEAT STABILITY</subject><subject>invertase</subject><subject>TEMPERATURE RESISTANCE</subject><subject>thermal inactivation</subject><subject>Thermodynamics</subject><subject>TREHALOSE</subject><issn>0022-1147</issn><issn>1750-3841</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><recordid>eNqVkUGP1CAUxxujiePqRzBpNl5boRQoXoy7uruajW4yu3okbyjdYaRlBKpTL351qZ3s3XeBR378HvmTZacYlTjV612JCaNFxSpcYiF4GTeoJrwpD4-yFeYUFaSp8eNshVBVFRjX_Gn2LIQdmnvCVtmf2632Pdg8RNgYa-KUuy43w0_tIwSddrnX7ah0W_TOhDh6nUPv_H7rxpD3EL1ROiyYhWjckEeX31sIYZqdMeFDm0evt2BdEio_pWNrze9_9PPsSQc26BfH9SS7u_hwe35VXH-5_Hj-7rpQtRC04FS3rEMNZg3TABvBuGJKcRDtpqk4nntRc9QAIi0nrAbNO4W0Ym0qgshJdrp49979GHWIcudGP6SREouUmODNDL1ZIOVdCF53cu9ND36SGMk5b7mTc95yzlvOectj3vKQLr86ToCgwHYeBmXCg6GiHFOBE_Z2wX4Zq6f_GCA_XbxfY0SToVgM6Tv04cEA_rtknHAqv32-lFdfz9bVWXMjbxL_cuE7cBLufXrU3Xp2o6ailJG_-PSwlQ</recordid><startdate>199701</startdate><enddate>199701</enddate><creator>Cardona, S. 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(Univ. de Buenos Aires, Buenos Aires, Argentina.)</creatorcontrib><creatorcontrib>Schebor, C</creatorcontrib><creatorcontrib>Buera, M.P</creatorcontrib><creatorcontrib>Karel, M</creatorcontrib><creatorcontrib>Chirife, J</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Toxicology Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Environment Abstracts</collection><jtitle>Journal of food science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cardona, S. 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However, at moisture contents which allowed trehalose crystallization rapid thermal inactivation of invertase was observed. Invertase inactivation in heated PVP, MD and trehalose systems of reduced-moisture could not be predicted on the basis of glass transition and this was particularly true for trehalose. Conditions which would allow collapse of the systems and crystallization of trehalose were fairly well predicted based on the estimated T(g) of model systems</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><doi>10.1111/j.1365-2621.1997.tb04378.x</doi><tpages>8</tpages></addata></record> |
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subjects | Biological and medical sciences CRYSTALLIZATION Enzymes Food engineering Food industries Food science Fundamental and applied biological sciences. Psychology General aspects GLASS TRANSITION HEAT HEAT STABILITY invertase TEMPERATURE RESISTANCE thermal inactivation Thermodynamics TREHALOSE |
title | Thermal stability of invertase in reduced-moisture amorphous matrices in relation to glassy state and trehalose crystallization |
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