Preparation and characterization of high-quality rice bran proteins
Rice bran contains 120-200 g kg-1 protein in addition to a large amount of fat, carbohydrate, and phytic acid. Rice bran protein (RBP) fractions were refined by a two-step preparation to eliminate residual carbohydrate. The first step involved the sequential extraction of defatted rice bran into RBP...
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| Veröffentlicht in: | Journal of the science of food and agriculture 2007-05, Vol.87 (7), p.1219-1227 |
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| creator | Adebiyi, A.P Adebiyi, A.O Ogawa, T Muramoto, K |
| description | Rice bran contains 120-200 g kg-1 protein in addition to a large amount of fat, carbohydrate, and phytic acid. Rice bran protein (RBP) fractions were refined by a two-step preparation to eliminate residual carbohydrate. The first step involved the sequential extraction of defatted rice bran into RBP fractions using their distinct solubility to give 37 g kg-1 of albumin, 31 g kg-1 of globulin, 27 g kg-1 of glutelin, and 2 g kg-1 of prolamin. In the second step, carried out by dissolving in respective solvent and isoelectric precipitation, the protein content of each fraction increased from 69% to 97% for albumin, from 71% to 90% for globulin, from 74% to 83% for glutelin, and from 18% to 20% for prolamin. The low protein content in the prolamin fraction might be due to its low solubility in the protein assay. Emulsifying stability index and surface hydrophobicity increased in the second-step preparation of albumin and globulin, but not of glutelin. Emulsifying properties of RBPs were lower than that of a soybean protein isolate. Denaturation temperatures and enthalpy values of denaturation for albumin, globulin, glutelin, and prolamin were 50.1 °C/1.2 J g-1, 79.0 °C/1.8 J g-1, 74.5 °C/3.0 J g-1, and 78.5 °C/8.1 J g-1, respectively. No significant differences in the denaturation temperatures and enthalpy values of denaturation of RBP fractions were obtained with these two-step preparations (P < 0.05). |
| doi_str_mv | 10.1002/jsfa.2819 |
| format | Article |
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Rice bran protein (RBP) fractions were refined by a two-step preparation to eliminate residual carbohydrate. The first step involved the sequential extraction of defatted rice bran into RBP fractions using their distinct solubility to give 37 g kg-1 of albumin, 31 g kg-1 of globulin, 27 g kg-1 of glutelin, and 2 g kg-1 of prolamin. In the second step, carried out by dissolving in respective solvent and isoelectric precipitation, the protein content of each fraction increased from 69% to 97% for albumin, from 71% to 90% for globulin, from 74% to 83% for glutelin, and from 18% to 20% for prolamin. The low protein content in the prolamin fraction might be due to its low solubility in the protein assay. Emulsifying stability index and surface hydrophobicity increased in the second-step preparation of albumin and globulin, but not of glutelin. Emulsifying properties of RBPs were lower than that of a soybean protein isolate. Denaturation temperatures and enthalpy values of denaturation for albumin, globulin, glutelin, and prolamin were 50.1 °C/1.2 J g-1, 79.0 °C/1.8 J g-1, 74.5 °C/3.0 J g-1, and 78.5 °C/8.1 J g-1, respectively. No significant differences in the denaturation temperatures and enthalpy values of denaturation of RBP fractions were obtained with these two-step preparations (P < 0.05).</description><identifier>ISSN: 0022-5142</identifier><identifier>EISSN: 1097-0010</identifier><identifier>DOI: 10.1002/jsfa.2819</identifier><identifier>CODEN: JSFAAE</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>albumins ; amino acid composition ; Biological and medical sciences ; carbohydrate content ; Carbohydrates ; defatting ; denaturation ; emulsifying properties ; emulsifying property ; Food industries ; Food science ; Fundamental and applied biological sciences. Psychology ; globulins ; glutelins ; high-quality rice bran proteins ; lipid content ; phytic acid ; prolamins ; protein content ; protein quality ; Proteins ; Rice ; rice bran ; rice bran protein ; rice protein ; solubility ; soy protein</subject><ispartof>Journal of the science of food and agriculture, 2007-05, Vol.87 (7), p.1219-1227</ispartof><rights>Copyright © 2007 Society of Chemical Industry</rights><rights>2007 INIST-CNRS</rights><rights>Copyright John Wiley and Sons, Limited May 2007</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4199-ac07a469a9d1b128b14d5a9ed7525d31e9f6d7caafb6e2e6f0cb93028c89ec883</citedby><cites>FETCH-LOGICAL-c4199-ac07a469a9d1b128b14d5a9ed7525d31e9f6d7caafb6e2e6f0cb93028c89ec883</cites></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.2819$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjsfa.2819$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18711505$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Adebiyi, A.P</creatorcontrib><creatorcontrib>Adebiyi, A.O</creatorcontrib><creatorcontrib>Ogawa, T</creatorcontrib><creatorcontrib>Muramoto, K</creatorcontrib><title>Preparation and characterization of high-quality rice bran proteins</title><title>Journal of the science of food and agriculture</title><addtitle>J. Sci. Food Agric</addtitle><description>Rice bran contains 120-200 g kg-1 protein in addition to a large amount of fat, carbohydrate, and phytic acid. Rice bran protein (RBP) fractions were refined by a two-step preparation to eliminate residual carbohydrate. The first step involved the sequential extraction of defatted rice bran into RBP fractions using their distinct solubility to give 37 g kg-1 of albumin, 31 g kg-1 of globulin, 27 g kg-1 of glutelin, and 2 g kg-1 of prolamin. In the second step, carried out by dissolving in respective solvent and isoelectric precipitation, the protein content of each fraction increased from 69% to 97% for albumin, from 71% to 90% for globulin, from 74% to 83% for glutelin, and from 18% to 20% for prolamin. The low protein content in the prolamin fraction might be due to its low solubility in the protein assay. Emulsifying stability index and surface hydrophobicity increased in the second-step preparation of albumin and globulin, but not of glutelin. Emulsifying properties of RBPs were lower than that of a soybean protein isolate. Denaturation temperatures and enthalpy values of denaturation for albumin, globulin, glutelin, and prolamin were 50.1 °C/1.2 J g-1, 79.0 °C/1.8 J g-1, 74.5 °C/3.0 J g-1, and 78.5 °C/8.1 J g-1, respectively. No significant differences in the denaturation temperatures and enthalpy values of denaturation of RBP fractions were obtained with these two-step preparations (P < 0.05).</description><subject>albumins</subject><subject>amino acid composition</subject><subject>Biological and medical sciences</subject><subject>carbohydrate content</subject><subject>Carbohydrates</subject><subject>defatting</subject><subject>denaturation</subject><subject>emulsifying properties</subject><subject>emulsifying property</subject><subject>Food industries</subject><subject>Food science</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>globulins</subject><subject>glutelins</subject><subject>high-quality rice bran proteins</subject><subject>lipid content</subject><subject>phytic acid</subject><subject>prolamins</subject><subject>protein content</subject><subject>protein quality</subject><subject>Proteins</subject><subject>Rice</subject><subject>rice bran</subject><subject>rice bran protein</subject><subject>rice protein</subject><subject>solubility</subject><subject>soy protein</subject><issn>0022-5142</issn><issn>1097-0010</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><recordid>eNp1kFFP2zAUha1pSCuMB34BEdIm8RC4dhLHfkQdsA00EG01aS_WjWNTdyEpdirofj2uUoGENN0H69rfOff6EHJA4YQCsNNFsHjCBJUfyIiCLFMACh_JKL6xtKA5-0R2Q1gAgJScj8j41psleuxd1ybY1omex073xrt_w2Vnk7m7n6ePK2xcv0680yapPLbJ0ne9cW34THYsNsHsb889Mrs4n46_p9c3lz_GZ9epzqmUKWooMecSZU0rykRF87pAaeqyYEWdUSMtr0uNaCtumOEWdCUzYEILabQQ2R75OvjGwY8rE3r14II2TYOt6VZBMSliyTyCR-_ARbfybdxNMcZ4mUvJInQ8QNp3IXhj1dK7B_RrRUFtslSbLNUmy8h-2Rpi0NjY-HvtwptAlJQWUETudOCeXGPW_zdUPycXZ1vndFC40JvnVwX6v4qXWVmo378u1ZSNv02v7v6oTQaHA2-xU3jv4xazCQOaAQjOBM-zF-qqm5E</recordid><startdate>200705</startdate><enddate>200705</enddate><creator>Adebiyi, A.P</creator><creator>Adebiyi, A.O</creator><creator>Ogawa, T</creator><creator>Muramoto, K</creator><general>John Wiley & Sons, Ltd</general><general>Wiley</general><general>John Wiley and Sons, Limited</general><scope>FBQ</scope><scope>BSCLL</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</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></search><sort><creationdate>200705</creationdate><title>Preparation and characterization of high-quality rice bran proteins</title><author>Adebiyi, A.P ; Adebiyi, A.O ; Ogawa, T ; Muramoto, K</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4199-ac07a469a9d1b128b14d5a9ed7525d31e9f6d7caafb6e2e6f0cb93028c89ec883</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>albumins</topic><topic>amino acid composition</topic><topic>Biological and medical sciences</topic><topic>carbohydrate content</topic><topic>Carbohydrates</topic><topic>defatting</topic><topic>denaturation</topic><topic>emulsifying properties</topic><topic>emulsifying property</topic><topic>Food industries</topic><topic>Food science</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>globulins</topic><topic>glutelins</topic><topic>high-quality rice bran proteins</topic><topic>lipid content</topic><topic>phytic acid</topic><topic>prolamins</topic><topic>protein content</topic><topic>protein quality</topic><topic>Proteins</topic><topic>Rice</topic><topic>rice bran</topic><topic>rice bran protein</topic><topic>rice protein</topic><topic>solubility</topic><topic>soy protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Adebiyi, A.P</creatorcontrib><creatorcontrib>Adebiyi, A.O</creatorcontrib><creatorcontrib>Ogawa, T</creatorcontrib><creatorcontrib>Muramoto, K</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Pascal-Francis</collection><collection>CrossRef</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><jtitle>Journal of the science of food and agriculture</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Adebiyi, A.P</au><au>Adebiyi, A.O</au><au>Ogawa, T</au><au>Muramoto, K</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Preparation and characterization of high-quality rice bran proteins</atitle><jtitle>Journal of the science of food and agriculture</jtitle><addtitle>J. Sci. Food Agric</addtitle><date>2007-05</date><risdate>2007</risdate><volume>87</volume><issue>7</issue><spage>1219</spage><epage>1227</epage><pages>1219-1227</pages><issn>0022-5142</issn><eissn>1097-0010</eissn><coden>JSFAAE</coden><abstract>Rice bran contains 120-200 g kg-1 protein in addition to a large amount of fat, carbohydrate, and phytic acid. Rice bran protein (RBP) fractions were refined by a two-step preparation to eliminate residual carbohydrate. The first step involved the sequential extraction of defatted rice bran into RBP fractions using their distinct solubility to give 37 g kg-1 of albumin, 31 g kg-1 of globulin, 27 g kg-1 of glutelin, and 2 g kg-1 of prolamin. In the second step, carried out by dissolving in respective solvent and isoelectric precipitation, the protein content of each fraction increased from 69% to 97% for albumin, from 71% to 90% for globulin, from 74% to 83% for glutelin, and from 18% to 20% for prolamin. The low protein content in the prolamin fraction might be due to its low solubility in the protein assay. Emulsifying stability index and surface hydrophobicity increased in the second-step preparation of albumin and globulin, but not of glutelin. Emulsifying properties of RBPs were lower than that of a soybean protein isolate. Denaturation temperatures and enthalpy values of denaturation for albumin, globulin, glutelin, and prolamin were 50.1 °C/1.2 J g-1, 79.0 °C/1.8 J g-1, 74.5 °C/3.0 J g-1, and 78.5 °C/8.1 J g-1, respectively. No significant differences in the denaturation temperatures and enthalpy values of denaturation of RBP fractions were obtained with these two-step preparations (P < 0.05).</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><doi>10.1002/jsfa.2819</doi><tpages>9</tpages></addata></record> |
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| subjects | albumins amino acid composition Biological and medical sciences carbohydrate content Carbohydrates defatting denaturation emulsifying properties emulsifying property Food industries Food science Fundamental and applied biological sciences. Psychology globulins glutelins high-quality rice bran proteins lipid content phytic acid prolamins protein content protein quality Proteins Rice rice bran rice bran protein rice protein solubility soy protein |
| title | Preparation and characterization of high-quality rice bran proteins |
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