The effects of surface adsorption on the thermal stability of proteins
The effect of surface adsorption on the structure and stability of proteins is a matter of increasing interest in biotechnology. Therefore, we have examined the effect of adsorption to silica on the thermal stability of 7 proteins employing differential scanning calorimetry (DSC) and front surface f...
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Veröffentlicht in: | Biotechnology and bioengineering 1992-06, Vol.40 (1), p.8-15 |
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creator | Steadman, Bryan L. Thompson, Karen C. Middaugh, C. Russell Matsuno, Ken Vrona, Susan Lawson, Erlinda Q. Lewis, Randolph V. |
description | The effect of surface adsorption on the structure and stability of proteins is a matter of increasing interest in biotechnology. Therefore, we have examined the effect of adsorption to silica on the thermal stability of 7 proteins employing differential scanning calorimetry (DSC) and front surface fluorescence (FSF) spectroscopy. In general, it was found that surface adsorption decreased the thermal stability of the bound protein. Using lysozyme for further studies, DSC, FSF, and FTIR spectroscopies, as well as enzymatic activity measurements, were used to explore the effect of decreasing surface apolarity on stability. It was observed that increasing surface apolarity produced decreasing stability and increasing structural alteration of the adsorbed protein. |
doi_str_mv | 10.1002/bit.260400103 |
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Russell ; Matsuno, Ken ; Vrona, Susan ; Lawson, Erlinda Q. ; Lewis, Randolph V.</creator><creatorcontrib>Steadman, Bryan L. ; Thompson, Karen C. ; Middaugh, C. Russell ; Matsuno, Ken ; Vrona, Susan ; Lawson, Erlinda Q. ; Lewis, Randolph V.</creatorcontrib><description>The effect of surface adsorption on the structure and stability of proteins is a matter of increasing interest in biotechnology. Therefore, we have examined the effect of adsorption to silica on the thermal stability of 7 proteins employing differential scanning calorimetry (DSC) and front surface fluorescence (FSF) spectroscopy. In general, it was found that surface adsorption decreased the thermal stability of the bound protein. Using lysozyme for further studies, DSC, FSF, and FTIR spectroscopies, as well as enzymatic activity measurements, were used to explore the effect of decreasing surface apolarity on stability. It was observed that increasing surface apolarity produced decreasing stability and increasing structural alteration of the adsorbed protein.</description><identifier>ISSN: 0006-3592</identifier><identifier>EISSN: 1097-0290</identifier><identifier>DOI: 10.1002/bit.260400103</identifier><identifier>PMID: 18601038</identifier><identifier>CODEN: BIBIAU</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>adsorption ; Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Fundamental and applied biological sciences. 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Using lysozyme for further studies, DSC, FSF, and FTIR spectroscopies, as well as enzymatic activity measurements, were used to explore the effect of decreasing surface apolarity on stability. It was observed that increasing surface apolarity produced decreasing stability and increasing structural alteration of the adsorbed protein.</description><subject>adsorption</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General aspects, investigation methods</subject><subject>I.R. spectroscopy</subject><subject>lysozyme</subject><subject>protein stability</subject><subject>Proteins</subject><subject>silica</subject><subject>stability</subject><subject>surface polarity</subject><issn>0006-3592</issn><issn>1097-0290</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><recordid>eNp90E1vEzEQBmALUdG0cOSK9oDoact4_bU-QtSGohSEFMTRmvXawrDJprYjmn-Po6wCp0q2LEuPZ8YvIa8pXFOA5n0X8nUjgQNQYM_IjIJWNTQanpMZAMiaCd2ck4uUfpWraqV8Qc5pKw-8nZHb1U9XOe-dzakafZV20aN1FfZpjNscxk1VVi6o7LjGoUoZuzCEvD_wbRyzC5v0kpx5HJJ7NZ2X5PvtzWr-qV5-XdzNPyxry1XDag-WY8td36seFSrfSt76TpQPiJY5ELrTKB1zHYe-72VnlWACkXEQkmtkl-TqWLc0fti5lM06JOuGATdu3CWjGGsYFZoW-e5JSSXTQui2wPoIbRxTis6bbQxrjHtDwRwiNiVic4q4-DdT4V23dv0_PWVawNsJYLI4-IgbG9LJCQ5Uq8OA6sj-hMHtn25qPt6t_p9gmjik7B5PLzH-NlIxJcyPLwuz4N-W96vP3MzZX7rDol8</recordid><startdate>19920605</startdate><enddate>19920605</enddate><creator>Steadman, Bryan L.</creator><creator>Thompson, Karen C.</creator><creator>Middaugh, C. 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Psychology</topic><topic>General aspects, investigation methods</topic><topic>I.R. spectroscopy</topic><topic>lysozyme</topic><topic>protein stability</topic><topic>Proteins</topic><topic>silica</topic><topic>stability</topic><topic>surface polarity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Steadman, Bryan L.</creatorcontrib><creatorcontrib>Thompson, Karen C.</creatorcontrib><creatorcontrib>Middaugh, C. 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Using lysozyme for further studies, DSC, FSF, and FTIR spectroscopies, as well as enzymatic activity measurements, were used to explore the effect of decreasing surface apolarity on stability. It was observed that increasing surface apolarity produced decreasing stability and increasing structural alteration of the adsorbed protein.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>18601038</pmid><doi>10.1002/bit.260400103</doi><tpages>8</tpages></addata></record> |
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subjects | adsorption Analytical, structural and metabolic biochemistry Biological and medical sciences Fundamental and applied biological sciences. Psychology General aspects, investigation methods I.R. spectroscopy lysozyme protein stability Proteins silica stability surface polarity |
title | The effects of surface adsorption on the thermal stability of proteins |
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