Some characteristics and functional properties of rapeseed protein prepared by ultrasonication, ultrafiltration and isoelectric precipitation
BACKGROUND: The presence of complex protein constituents and difficulties in extracting protein from rapeseed meal limit the application of rapeseed protein in food processing. However, double‐low rapeseed (low erucic acid, low glucosinolate) protein is a type of complete protein that is of potentia...
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| Veröffentlicht in: | Journal of the science of food and agriculture 2011-06, Vol.91 (8), p.1488-1498 |
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| creator | Dong, Xu-Yan Guo, Lu-Lu Wei, Fang Li, Ju-Fang Jiang, Mu-Lan Li, Guang-Ming Zhao, Yuan-Di Chen, Hong |
| description | BACKGROUND: The presence of complex protein constituents and difficulties in extracting protein from rapeseed meal limit the application of rapeseed protein in food processing. However, double‐low rapeseed (low erucic acid, low glucosinolate) protein is a type of complete protein that is of potential use in the food industry. In this study the characteristics and functional properties of rapeseed protein prepared by ultrasonic‐assisted extraction, ultrafiltration and isoelectric precipitation were analysed and compared with those of soybean protein.
RESULTS: The extraction efficiency with the ultrasonic‐assisted method was significantly higher than that obtained with the traditional method. Ultrafiltration and isoelectric precipitation yielded three different proteins: ultrafiltered protein RPs and precipitated proteins RP5.8 and RP3.6. Chromatographic separation of RPs resulted in four fractions: RPsI, RPsII, RPsIII and RPsIV. The distribution of the isoelectric point of rapeseed protein was investigated by two‐dimensional electrophoresis. The amino acid composition of RPs renders it suitable for human consumption. The hydrophobic/hydrophilic amino acid ratio of rapeseed protein was higher than that of soybean protein. The functional properties (oil adsorption ability, emulsifying capacity, foaming capacity and foam stability) of RPs, RP5.8 and RP3.6 were found to be better than those of soybean protein.
CONCLUSION: Ultrasonication and ultrafiltration were significantly better than the traditional method of rapeseed protein extraction. The ultrafiltered rapeseed protein RPs had superior functional properties. The results of this study provide useful indicators for rapeseed protein as a potential replacement for other proteins. Copyright © 2011 Society of Chemical Industry |
| doi_str_mv | 10.1002/jsfa.4339 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_864961404</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2350589141</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4189-d59c41aa0ed1fbf85aceea316858ae489a9a8c4d343b6c457800761ecaf8b16d3</originalsourceid><addsrcrecordid>eNp9ks1u1DAQxy0EokvhwAugCAnRA2nt2HHsY1nRhVLBoXwcrYkzEV6ySWonavcheOfa3W2ROHDxjGZ-_7E9M4S8ZPSYUVqcrEMLx4Jz_YgsGNVVTimjj8ki5oq8ZKI4IM9CWFNKtZbyKTkoGFeCq2JB_lwOG8zsL_BgJ_QuTM6GDPoma-feTm7ooctGP4zoJ4chG9rMw4gBsUnhCV0fLY7gY6DeZnM3eQhD7ywk8btdoHXpTIG70i4M2KGdvLNJbN3oprvsc_KkhS7gi709JN_PPnxbfswvvq4-LU8vciuY0nlT6ugAUGxYW7eqBIsInElVKkChNGhQVjRc8FpaUVaK0koytNCqmsmGH5K3u7rxC1czhslsXLDYddDjMAejpNCSCSoiefRfklGuZGy3VhF9_Q-6HmYf-5fqVVxWQsoIvdpDc73BxozebcBvzf1EIvBmD0Cw0LUeeuvCX04wWWqebjvZcdeuw-1DnlGTVsKklTBpJcz55dlpcqIi3ynikPHmQQH-t4nPq0rz88vKVLp8z38sP5sVvwXHBrsa</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>867367466</pqid></control><display><type>article</type><title>Some characteristics and functional properties of rapeseed protein prepared by ultrasonication, ultrafiltration and isoelectric precipitation</title><source>MEDLINE</source><source>Wiley Online Library Journals Frontfile Complete</source><creator>Dong, Xu-Yan ; Guo, Lu-Lu ; Wei, Fang ; Li, Ju-Fang ; Jiang, Mu-Lan ; Li, Guang-Ming ; Zhao, Yuan-Di ; Chen, Hong</creator><creatorcontrib>Dong, Xu-Yan ; Guo, Lu-Lu ; Wei, Fang ; Li, Ju-Fang ; Jiang, Mu-Lan ; Li, Guang-Ming ; Zhao, Yuan-Di ; Chen, Hong</creatorcontrib><description>BACKGROUND: The presence of complex protein constituents and difficulties in extracting protein from rapeseed meal limit the application of rapeseed protein in food processing. However, double‐low rapeseed (low erucic acid, low glucosinolate) protein is a type of complete protein that is of potential use in the food industry. In this study the characteristics and functional properties of rapeseed protein prepared by ultrasonic‐assisted extraction, ultrafiltration and isoelectric precipitation were analysed and compared with those of soybean protein.
RESULTS: The extraction efficiency with the ultrasonic‐assisted method was significantly higher than that obtained with the traditional method. Ultrafiltration and isoelectric precipitation yielded three different proteins: ultrafiltered protein RPs and precipitated proteins RP5.8 and RP3.6. Chromatographic separation of RPs resulted in four fractions: RPsI, RPsII, RPsIII and RPsIV. The distribution of the isoelectric point of rapeseed protein was investigated by two‐dimensional electrophoresis. The amino acid composition of RPs renders it suitable for human consumption. The hydrophobic/hydrophilic amino acid ratio of rapeseed protein was higher than that of soybean protein. The functional properties (oil adsorption ability, emulsifying capacity, foaming capacity and foam stability) of RPs, RP5.8 and RP3.6 were found to be better than those of soybean protein.
CONCLUSION: Ultrasonication and ultrafiltration were significantly better than the traditional method of rapeseed protein extraction. The ultrafiltered rapeseed protein RPs had superior functional properties. The results of this study provide useful indicators for rapeseed protein as a potential replacement for other proteins. Copyright © 2011 Society of Chemical Industry</description><identifier>ISSN: 0022-5142</identifier><identifier>ISSN: 1097-0010</identifier><identifier>EISSN: 1097-0010</identifier><identifier>DOI: 10.1002/jsfa.4339</identifier><identifier>PMID: 21384382</identifier><identifier>CODEN: JSFAAE</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Adsorption ; Amino acids ; Amino Acids - analysis ; Biological and medical sciences ; Brassica rapa - chemistry ; Chemical Precipitation ; Dietary Proteins - analysis ; Dietary Proteins - isolation & purification ; Emulsifying Agents ; Filtration - methods ; Food engineering ; Food Handling - methods ; Food industries ; Food science ; Functional foods & nutraceuticals ; functional properties ; Fundamental and applied biological sciences. Psychology ; General aspects ; Glycine max - chemistry ; Humans ; Hydrophobic and Hydrophilic Interactions ; Isoelectric Point ; isoelectric precipitation ; Plant Extracts - chemistry ; Plant Proteins - analysis ; Plant Proteins - chemistry ; Plant Proteins - isolation & purification ; Proteins ; Rape plants ; rapeseed protein ; Seeds ; Seeds - chemistry ; Sonication - methods ; Studies ; ultrafiltration ; ultrasonic-assisted extraction</subject><ispartof>Journal of the science of food and agriculture, 2011-06, Vol.91 (8), p.1488-1498</ispartof><rights>Copyright © 2011 Society of Chemical Industry</rights><rights>2015 INIST-CNRS</rights><rights>Copyright © 2011 Society of Chemical Industry.</rights><rights>Copyright John Wiley and Sons, Limited Jun 2011</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4189-d59c41aa0ed1fbf85aceea316858ae489a9a8c4d343b6c457800761ecaf8b16d3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjsfa.4339$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjsfa.4339$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,778,782,1414,27911,27912,45561,45562</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=24165938$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21384382$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dong, Xu-Yan</creatorcontrib><creatorcontrib>Guo, Lu-Lu</creatorcontrib><creatorcontrib>Wei, Fang</creatorcontrib><creatorcontrib>Li, Ju-Fang</creatorcontrib><creatorcontrib>Jiang, Mu-Lan</creatorcontrib><creatorcontrib>Li, Guang-Ming</creatorcontrib><creatorcontrib>Zhao, Yuan-Di</creatorcontrib><creatorcontrib>Chen, Hong</creatorcontrib><title>Some characteristics and functional properties of rapeseed protein prepared by ultrasonication, ultrafiltration and isoelectric precipitation</title><title>Journal of the science of food and agriculture</title><addtitle>J. Sci. Food Agric</addtitle><description>BACKGROUND: The presence of complex protein constituents and difficulties in extracting protein from rapeseed meal limit the application of rapeseed protein in food processing. However, double‐low rapeseed (low erucic acid, low glucosinolate) protein is a type of complete protein that is of potential use in the food industry. In this study the characteristics and functional properties of rapeseed protein prepared by ultrasonic‐assisted extraction, ultrafiltration and isoelectric precipitation were analysed and compared with those of soybean protein.
RESULTS: The extraction efficiency with the ultrasonic‐assisted method was significantly higher than that obtained with the traditional method. Ultrafiltration and isoelectric precipitation yielded three different proteins: ultrafiltered protein RPs and precipitated proteins RP5.8 and RP3.6. Chromatographic separation of RPs resulted in four fractions: RPsI, RPsII, RPsIII and RPsIV. The distribution of the isoelectric point of rapeseed protein was investigated by two‐dimensional electrophoresis. The amino acid composition of RPs renders it suitable for human consumption. The hydrophobic/hydrophilic amino acid ratio of rapeseed protein was higher than that of soybean protein. The functional properties (oil adsorption ability, emulsifying capacity, foaming capacity and foam stability) of RPs, RP5.8 and RP3.6 were found to be better than those of soybean protein.
CONCLUSION: Ultrasonication and ultrafiltration were significantly better than the traditional method of rapeseed protein extraction. The ultrafiltered rapeseed protein RPs had superior functional properties. The results of this study provide useful indicators for rapeseed protein as a potential replacement for other proteins. Copyright © 2011 Society of Chemical Industry</description><subject>Adsorption</subject><subject>Amino acids</subject><subject>Amino Acids - analysis</subject><subject>Biological and medical sciences</subject><subject>Brassica rapa - chemistry</subject><subject>Chemical Precipitation</subject><subject>Dietary Proteins - analysis</subject><subject>Dietary Proteins - isolation & purification</subject><subject>Emulsifying Agents</subject><subject>Filtration - methods</subject><subject>Food engineering</subject><subject>Food Handling - methods</subject><subject>Food industries</subject><subject>Food science</subject><subject>Functional foods & nutraceuticals</subject><subject>functional properties</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General aspects</subject><subject>Glycine max - chemistry</subject><subject>Humans</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Isoelectric Point</subject><subject>isoelectric precipitation</subject><subject>Plant Extracts - chemistry</subject><subject>Plant Proteins - analysis</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - isolation & purification</subject><subject>Proteins</subject><subject>Rape plants</subject><subject>rapeseed protein</subject><subject>Seeds</subject><subject>Seeds - chemistry</subject><subject>Sonication - methods</subject><subject>Studies</subject><subject>ultrafiltration</subject><subject>ultrasonic-assisted extraction</subject><issn>0022-5142</issn><issn>1097-0010</issn><issn>1097-0010</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9ks1u1DAQxy0EokvhwAugCAnRA2nt2HHsY1nRhVLBoXwcrYkzEV6ySWonavcheOfa3W2ROHDxjGZ-_7E9M4S8ZPSYUVqcrEMLx4Jz_YgsGNVVTimjj8ki5oq8ZKI4IM9CWFNKtZbyKTkoGFeCq2JB_lwOG8zsL_BgJ_QuTM6GDPoma-feTm7ooctGP4zoJ4chG9rMw4gBsUnhCV0fLY7gY6DeZnM3eQhD7ywk8btdoHXpTIG70i4M2KGdvLNJbN3oprvsc_KkhS7gi709JN_PPnxbfswvvq4-LU8vciuY0nlT6ugAUGxYW7eqBIsInElVKkChNGhQVjRc8FpaUVaK0koytNCqmsmGH5K3u7rxC1czhslsXLDYddDjMAejpNCSCSoiefRfklGuZGy3VhF9_Q-6HmYf-5fqVVxWQsoIvdpDc73BxozebcBvzf1EIvBmD0Cw0LUeeuvCX04wWWqebjvZcdeuw-1DnlGTVsKklTBpJcz55dlpcqIi3ynikPHmQQH-t4nPq0rz88vKVLp8z38sP5sVvwXHBrsa</recordid><startdate>201106</startdate><enddate>201106</enddate><creator>Dong, Xu-Yan</creator><creator>Guo, Lu-Lu</creator><creator>Wei, Fang</creator><creator>Li, Ju-Fang</creator><creator>Jiang, Mu-Lan</creator><creator>Li, Guang-Ming</creator><creator>Zhao, Yuan-Di</creator><creator>Chen, Hong</creator><general>John Wiley & Sons, Ltd</general><general>Wiley</general><general>John Wiley and Sons, Limited</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QF</scope><scope>7QL</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7ST</scope><scope>7T5</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>M7N</scope><scope>P64</scope><scope>SOI</scope><scope>7TG</scope><scope>KL.</scope><scope>7X8</scope></search><sort><creationdate>201106</creationdate><title>Some characteristics and functional properties of rapeseed protein prepared by ultrasonication, ultrafiltration and isoelectric precipitation</title><author>Dong, Xu-Yan ; Guo, Lu-Lu ; Wei, Fang ; Li, Ju-Fang ; Jiang, Mu-Lan ; Li, Guang-Ming ; Zhao, Yuan-Di ; Chen, Hong</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4189-d59c41aa0ed1fbf85aceea316858ae489a9a8c4d343b6c457800761ecaf8b16d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Adsorption</topic><topic>Amino acids</topic><topic>Amino Acids - analysis</topic><topic>Biological and medical sciences</topic><topic>Brassica rapa - chemistry</topic><topic>Chemical Precipitation</topic><topic>Dietary Proteins - analysis</topic><topic>Dietary Proteins - isolation & purification</topic><topic>Emulsifying Agents</topic><topic>Filtration - methods</topic><topic>Food engineering</topic><topic>Food Handling - methods</topic><topic>Food industries</topic><topic>Food science</topic><topic>Functional foods & nutraceuticals</topic><topic>functional properties</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General aspects</topic><topic>Glycine max - chemistry</topic><topic>Humans</topic><topic>Hydrophobic and Hydrophilic Interactions</topic><topic>Isoelectric Point</topic><topic>isoelectric precipitation</topic><topic>Plant Extracts - chemistry</topic><topic>Plant Proteins - analysis</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - isolation & purification</topic><topic>Proteins</topic><topic>Rape plants</topic><topic>rapeseed protein</topic><topic>Seeds</topic><topic>Seeds - chemistry</topic><topic>Sonication - methods</topic><topic>Studies</topic><topic>ultrafiltration</topic><topic>ultrasonic-assisted extraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dong, Xu-Yan</creatorcontrib><creatorcontrib>Guo, Lu-Lu</creatorcontrib><creatorcontrib>Wei, Fang</creatorcontrib><creatorcontrib>Li, Ju-Fang</creatorcontrib><creatorcontrib>Jiang, Mu-Lan</creatorcontrib><creatorcontrib>Li, Guang-Ming</creatorcontrib><creatorcontrib>Zhao, Yuan-Di</creatorcontrib><creatorcontrib>Chen, Hong</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Aluminium Industry Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Ceramic Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Ecology Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Environment Abstracts</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Materials Business File</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>METADEX</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>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environment Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts - Academic</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of the science of food and agriculture</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dong, Xu-Yan</au><au>Guo, Lu-Lu</au><au>Wei, Fang</au><au>Li, Ju-Fang</au><au>Jiang, Mu-Lan</au><au>Li, Guang-Ming</au><au>Zhao, Yuan-Di</au><au>Chen, Hong</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Some characteristics and functional properties of rapeseed protein prepared by ultrasonication, ultrafiltration and isoelectric precipitation</atitle><jtitle>Journal of the science of food and agriculture</jtitle><addtitle>J. Sci. Food Agric</addtitle><date>2011-06</date><risdate>2011</risdate><volume>91</volume><issue>8</issue><spage>1488</spage><epage>1498</epage><pages>1488-1498</pages><issn>0022-5142</issn><issn>1097-0010</issn><eissn>1097-0010</eissn><coden>JSFAAE</coden><abstract>BACKGROUND: The presence of complex protein constituents and difficulties in extracting protein from rapeseed meal limit the application of rapeseed protein in food processing. However, double‐low rapeseed (low erucic acid, low glucosinolate) protein is a type of complete protein that is of potential use in the food industry. In this study the characteristics and functional properties of rapeseed protein prepared by ultrasonic‐assisted extraction, ultrafiltration and isoelectric precipitation were analysed and compared with those of soybean protein.
RESULTS: The extraction efficiency with the ultrasonic‐assisted method was significantly higher than that obtained with the traditional method. Ultrafiltration and isoelectric precipitation yielded three different proteins: ultrafiltered protein RPs and precipitated proteins RP5.8 and RP3.6. Chromatographic separation of RPs resulted in four fractions: RPsI, RPsII, RPsIII and RPsIV. The distribution of the isoelectric point of rapeseed protein was investigated by two‐dimensional electrophoresis. The amino acid composition of RPs renders it suitable for human consumption. The hydrophobic/hydrophilic amino acid ratio of rapeseed protein was higher than that of soybean protein. The functional properties (oil adsorption ability, emulsifying capacity, foaming capacity and foam stability) of RPs, RP5.8 and RP3.6 were found to be better than those of soybean protein.
CONCLUSION: Ultrasonication and ultrafiltration were significantly better than the traditional method of rapeseed protein extraction. The ultrafiltered rapeseed protein RPs had superior functional properties. The results of this study provide useful indicators for rapeseed protein as a potential replacement for other proteins. Copyright © 2011 Society of Chemical Industry</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>21384382</pmid><doi>10.1002/jsfa.4339</doi><tpages>11</tpages></addata></record> |
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| subjects | Adsorption Amino acids Amino Acids - analysis Biological and medical sciences Brassica rapa - chemistry Chemical Precipitation Dietary Proteins - analysis Dietary Proteins - isolation & purification Emulsifying Agents Filtration - methods Food engineering Food Handling - methods Food industries Food science Functional foods & nutraceuticals functional properties Fundamental and applied biological sciences. Psychology General aspects Glycine max - chemistry Humans Hydrophobic and Hydrophilic Interactions Isoelectric Point isoelectric precipitation Plant Extracts - chemistry Plant Proteins - analysis Plant Proteins - chemistry Plant Proteins - isolation & purification Proteins Rape plants rapeseed protein Seeds Seeds - chemistry Sonication - methods Studies ultrafiltration ultrasonic-assisted extraction |
| title | Some characteristics and functional properties of rapeseed protein prepared by ultrasonication, ultrafiltration and isoelectric precipitation |
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