Combined microwave and enzymatic treatments for β-lactoglobulin and bovine whey proteins and their effect on the IgE immunoreactivity
Effect of combined microwave (MW) and enzymatic hydrolysis on the human immunoglobulin E (IgE)-binding properties of β-lactoglobulin (β-lg) and other whey proteins (WP) was investigated. Separated β-lg and full whey protein isolate (WPI) were hydrolyzed with trypsin, chymotrypsin, mixture of trypsin...
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Veröffentlicht in: | European food research & technology 2011-11, Vol.233 (5), p.859-867 |
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creator | El Mecherfi, Kamel Eddine Saidi, Djamel Kheroua, Omar Boudraa, Ghazalia Touhami, Mahmoud Rouaud, Olivier Curet, Sébastien Choiset, Yvan Rabesona, Hanitra Chobert, Jean-Marc Haertlé, Thomas |
description | Effect of combined microwave (MW) and enzymatic hydrolysis on the human immunoglobulin E (IgE)-binding properties of β-lactoglobulin (β-lg) and other whey proteins (WP) was investigated. Separated β-lg and full whey protein isolate (WPI) were hydrolyzed with trypsin, chymotrypsin, mixture of trypsin/chymotrypsin, and pepsin at three microwave power levels: 50 W during 1 and 5 min, 100 and 200 W during 1 and 3 min. The immunoreactivity of the obtained hydrolysates resulting from combined microwave protease treatment was assessed using sera of young patients allergic to bovine whey proteins. The application of microwave treatment at 200 W enhances the hydrolysis of β-lg by pepsin in 3 min and decreases significantly its immunoreactivity. The extensive hydrolysis of the microwave-treated β-lg and WPI with trypsin, chymotrypsin, and the mixture of trypsin with chymotrypsin did not have an impact on the IgE binding of the products obtained in all the studied conditions. |
doi_str_mv | 10.1007/s00217-011-1581-y |
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Separated β-lg and full whey protein isolate (WPI) were hydrolyzed with trypsin, chymotrypsin, mixture of trypsin/chymotrypsin, and pepsin at three microwave power levels: 50 W during 1 and 5 min, 100 and 200 W during 1 and 3 min. The immunoreactivity of the obtained hydrolysates resulting from combined microwave protease treatment was assessed using sera of young patients allergic to bovine whey proteins. The application of microwave treatment at 200 W enhances the hydrolysis of β-lg by pepsin in 3 min and decreases significantly its immunoreactivity. The extensive hydrolysis of the microwave-treated β-lg and WPI with trypsin, chymotrypsin, and the mixture of trypsin with chymotrypsin did not have an impact on the IgE binding of the products obtained in all the studied conditions.</description><identifier>ISSN: 1438-2377</identifier><identifier>EISSN: 1438-2385</identifier><identifier>DOI: 10.1007/s00217-011-1581-y</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer-Verlag</publisher><subject>Agriculture ; Analytical Chemistry ; beta -lactoglobulin ; Biological and medical sciences ; Biotechnology ; Chemical and Process Engineering ; Chemistry ; Chemistry and Materials Science ; Chymotrypsin ; Engineering Sciences ; Food engineering ; Food industries ; Food Science ; Forestry ; Fundamental and applied biological sciences. Psychology ; Hydrolysates ; Hydrolysis ; Immunoglobulin E ; Immunoreactivity ; Life Sciences ; Milk and cheese industries. 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Separated β-lg and full whey protein isolate (WPI) were hydrolyzed with trypsin, chymotrypsin, mixture of trypsin/chymotrypsin, and pepsin at three microwave power levels: 50 W during 1 and 5 min, 100 and 200 W during 1 and 3 min. The immunoreactivity of the obtained hydrolysates resulting from combined microwave protease treatment was assessed using sera of young patients allergic to bovine whey proteins. The application of microwave treatment at 200 W enhances the hydrolysis of β-lg by pepsin in 3 min and decreases significantly its immunoreactivity. The extensive hydrolysis of the microwave-treated β-lg and WPI with trypsin, chymotrypsin, and the mixture of trypsin with chymotrypsin did not have an impact on the IgE binding of the products obtained in all the studied conditions.</description><subject>Agriculture</subject><subject>Analytical Chemistry</subject><subject>beta -lactoglobulin</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Chemical and Process Engineering</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Chymotrypsin</subject><subject>Engineering Sciences</subject><subject>Food engineering</subject><subject>Food industries</subject><subject>Food Science</subject><subject>Forestry</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrolysates</subject><subject>Hydrolysis</subject><subject>Immunoglobulin E</subject><subject>Immunoreactivity</subject><subject>Life Sciences</subject><subject>Milk and cheese industries. Ice creams</subject><subject>Original Paper</subject><subject>Pepsin A</subject><subject>Proteinase</subject><subject>Trypsin</subject><subject>whey protein</subject><issn>1438-2377</issn><issn>1438-2385</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><recordid>eNp9kcFu1DAQhqMKpJbCA_TmSyU4BGzHjrPHalVopZW4wNmaOJNdV4ldbGer9AF4IB6EZ8Jpqj1yGnv-fz5p5i-KK0Y_M0rVl0gpZ6qkjJVMNqycz4oLJqqm5FUj35zeSp0X72J8oFRuaiYuit9bP7bWYUdGa4J_giMScB1B9zyPkKwhKSCkEV2KpPeB_P1TDmCS3w--nQbrXtytP2YGeTrgTB6DT2hdfBHSAW0g2PdoEvFu-ZP7_S2x4zg5n8km2aNN8_vibQ9DxA-v9bL4-fX2x_au3H3_dr-92ZUmr5FKYJIq6KHCHkGhEapRuUjOwQhA2dW1MJI1lFPoWSdapG3VZZkC1krI6rL4tHIPMOjHYEcIs_Zg9d3NTi89ymuhNrQ6suz9uHrzRr8mjEmPNhocBnDop6gZ3VRC1JuGZytbrfmEMQbsT2xG9ZKPXvPROR-95KPnPHP9iodoYOgDOGPjaZALxRspFzZffTFLbo9BP_gpuHyl_8D_AZRTo2w</recordid><startdate>20111101</startdate><enddate>20111101</enddate><creator>El Mecherfi, Kamel Eddine</creator><creator>Saidi, Djamel</creator><creator>Kheroua, Omar</creator><creator>Boudraa, Ghazalia</creator><creator>Touhami, Mahmoud</creator><creator>Rouaud, Olivier</creator><creator>Curet, Sébastien</creator><creator>Choiset, Yvan</creator><creator>Rabesona, Hanitra</creator><creator>Chobert, Jean-Marc</creator><creator>Haertlé, Thomas</creator><general>Springer-Verlag</general><general>Springer</general><general>Springer Verlag (Germany)</general><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7T5</scope><scope>H94</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0003-1640-9954</orcidid><orcidid>https://orcid.org/0000-0001-6625-2903</orcidid></search><sort><creationdate>20111101</creationdate><title>Combined microwave and enzymatic treatments for β-lactoglobulin and bovine whey proteins and their effect on the IgE immunoreactivity</title><author>El Mecherfi, Kamel Eddine ; Saidi, Djamel ; Kheroua, Omar ; Boudraa, Ghazalia ; Touhami, Mahmoud ; Rouaud, Olivier ; Curet, Sébastien ; Choiset, Yvan ; Rabesona, Hanitra ; Chobert, Jean-Marc ; Haertlé, Thomas</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c385t-a1507afa3efea7ec47877ec522ac4ae5d664c518020af1d4be0b3d5220ae67453</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Agriculture</topic><topic>Analytical Chemistry</topic><topic>beta -lactoglobulin</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Chemical and Process Engineering</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Chymotrypsin</topic><topic>Engineering Sciences</topic><topic>Food engineering</topic><topic>Food industries</topic><topic>Food Science</topic><topic>Forestry</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrolysates</topic><topic>Hydrolysis</topic><topic>Immunoglobulin E</topic><topic>Immunoreactivity</topic><topic>Life Sciences</topic><topic>Milk and cheese industries. Ice creams</topic><topic>Original Paper</topic><topic>Pepsin A</topic><topic>Proteinase</topic><topic>Trypsin</topic><topic>whey protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>El Mecherfi, Kamel Eddine</creatorcontrib><creatorcontrib>Saidi, Djamel</creatorcontrib><creatorcontrib>Kheroua, Omar</creatorcontrib><creatorcontrib>Boudraa, Ghazalia</creatorcontrib><creatorcontrib>Touhami, Mahmoud</creatorcontrib><creatorcontrib>Rouaud, Olivier</creatorcontrib><creatorcontrib>Curet, Sébastien</creatorcontrib><creatorcontrib>Choiset, Yvan</creatorcontrib><creatorcontrib>Rabesona, Hanitra</creatorcontrib><creatorcontrib>Chobert, Jean-Marc</creatorcontrib><creatorcontrib>Haertlé, Thomas</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>European food research & technology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>El Mecherfi, Kamel Eddine</au><au>Saidi, Djamel</au><au>Kheroua, Omar</au><au>Boudraa, Ghazalia</au><au>Touhami, Mahmoud</au><au>Rouaud, Olivier</au><au>Curet, Sébastien</au><au>Choiset, Yvan</au><au>Rabesona, Hanitra</au><au>Chobert, Jean-Marc</au><au>Haertlé, Thomas</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Combined microwave and enzymatic treatments for β-lactoglobulin and bovine whey proteins and their effect on the IgE immunoreactivity</atitle><jtitle>European food research & technology</jtitle><stitle>Eur Food Res Technol</stitle><date>2011-11-01</date><risdate>2011</risdate><volume>233</volume><issue>5</issue><spage>859</spage><epage>867</epage><pages>859-867</pages><issn>1438-2377</issn><eissn>1438-2385</eissn><abstract>Effect of combined microwave (MW) and enzymatic hydrolysis on the human immunoglobulin E (IgE)-binding properties of β-lactoglobulin (β-lg) and other whey proteins (WP) was investigated. Separated β-lg and full whey protein isolate (WPI) were hydrolyzed with trypsin, chymotrypsin, mixture of trypsin/chymotrypsin, and pepsin at three microwave power levels: 50 W during 1 and 5 min, 100 and 200 W during 1 and 3 min. The immunoreactivity of the obtained hydrolysates resulting from combined microwave protease treatment was assessed using sera of young patients allergic to bovine whey proteins. The application of microwave treatment at 200 W enhances the hydrolysis of β-lg by pepsin in 3 min and decreases significantly its immunoreactivity. The extensive hydrolysis of the microwave-treated β-lg and WPI with trypsin, chymotrypsin, and the mixture of trypsin with chymotrypsin did not have an impact on the IgE binding of the products obtained in all the studied conditions.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer-Verlag</pub><doi>10.1007/s00217-011-1581-y</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0003-1640-9954</orcidid><orcidid>https://orcid.org/0000-0001-6625-2903</orcidid></addata></record> |
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subjects | Agriculture Analytical Chemistry beta -lactoglobulin Biological and medical sciences Biotechnology Chemical and Process Engineering Chemistry Chemistry and Materials Science Chymotrypsin Engineering Sciences Food engineering Food industries Food Science Forestry Fundamental and applied biological sciences. Psychology Hydrolysates Hydrolysis Immunoglobulin E Immunoreactivity Life Sciences Milk and cheese industries. Ice creams Original Paper Pepsin A Proteinase Trypsin whey protein |
title | Combined microwave and enzymatic treatments for β-lactoglobulin and bovine whey proteins and their effect on the IgE immunoreactivity |
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