Hydrophobicity, Solubility, and Emulsifying Properties of Enzyme-Modified Rice Endosperm Protein
Rice endosperm protein was modified to enhance solubility and emulsifying properties by controlled enzymatic hydrolysis. The optimum degree of hydrolysis (DH) was determined for acid, neutral, and alkaline type proteases. Solubility and emulsifying properties of the hydrolysates were compared and co...
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| Veröffentlicht in: | Cereal chemistry 2007-07, Vol.84 (4), p.343-349 |
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| creator | Paraman, I Hettiarachchy, N.S Schaefer, C Beck, M.I |
| description | Rice endosperm protein was modified to enhance solubility and emulsifying properties by controlled enzymatic hydrolysis. The optimum degree of hydrolysis (DH) was determined for acid, neutral, and alkaline type proteases. Solubility and emulsifying properties of the hydrolysates were compared and correlated with DH and surface hydrophobicity. DH was positively associated with solubility of resulting protein hydrolysate regardless of the hydrolyzing enzyme, but enzyme specificity and DH interactively determined the emulsifying properties of the protein hydrolysate. The optimum DH was 6-10% for good emulsifying properties of rice protein, depending on enzyme specificity. High hydrophobic and sulfhydryl disulfide (SH-SS) interactions contributed to protein insolubility even at high DH. The exposure of buried hydrophobic regions of protein that accompanied high-temperature enzyme inactivation promoted aggregation and cross-linking of partially hydrolyzed proteins, thus decreasing the solubility and emulsifying properties of the resulting hydrolysate. Due to the highly insoluble nature of rice protein, surface hydrophobicity was not a reliable indicator for predicting protein solubility and emulsifying properties. Solubility and molecular flexibility are the essential factors in achieving good emulsifying properties of rice endosperm protein isolates. |
| doi_str_mv | 10.1094/cchem-84-4-0343 |
| format | Article |
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The optimum degree of hydrolysis (DH) was determined for acid, neutral, and alkaline type proteases. Solubility and emulsifying properties of the hydrolysates were compared and correlated with DH and surface hydrophobicity. DH was positively associated with solubility of resulting protein hydrolysate regardless of the hydrolyzing enzyme, but enzyme specificity and DH interactively determined the emulsifying properties of the protein hydrolysate. The optimum DH was 6-10% for good emulsifying properties of rice protein, depending on enzyme specificity. High hydrophobic and sulfhydryl disulfide (SH-SS) interactions contributed to protein insolubility even at high DH. The exposure of buried hydrophobic regions of protein that accompanied high-temperature enzyme inactivation promoted aggregation and cross-linking of partially hydrolyzed proteins, thus decreasing the solubility and emulsifying properties of the resulting hydrolysate. Due to the highly insoluble nature of rice protein, surface hydrophobicity was not a reliable indicator for predicting protein solubility and emulsifying properties. Solubility and molecular flexibility are the essential factors in achieving good emulsifying properties of rice endosperm protein isolates.</description><identifier>ISSN: 0009-0352</identifier><identifier>EISSN: 1943-3638</identifier><identifier>DOI: 10.1094/cchem-84-4-0343</identifier><identifier>CODEN: CECHAF</identifier><language>eng</language><publisher>St. Paul, MN: The American Association of Cereal Chemists, Inc</publisher><subject>acid proteinases ; alkaline proteinases ; Biological and medical sciences ; Cereal and baking product industries ; chemical interactions ; degree of hydrolysis ; emulsifying properties ; endosperm ; enzymatic hydrolysis ; enzyme activity ; enzyme inactivation ; Food industries ; Fundamental and applied biological sciences. Psychology ; hydrophobic interactions ; hydrophobicity ; neutral proteinases ; protein aggregates ; protein hydrolysates ; protein-protein interactions ; proteinases ; rice ; rice protein ; solubility ; sulfhydryl groups</subject><ispartof>Cereal chemistry, 2007-07, Vol.84 (4), p.343-349</ispartof><rights>AACC International</rights><rights>2007 INIST-CNRS</rights><rights>Copyright American Association of Cereal Chemists Jul/Aug 2007</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4343-a3acfb6141893ff479c1d93e9b3729898844616bfda15b6c6d2a3598c24b0d653</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1094%2FCCHEM-84-4-0343$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1094%2FCCHEM-84-4-0343$$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=18999727$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Paraman, I</creatorcontrib><creatorcontrib>Hettiarachchy, N.S</creatorcontrib><creatorcontrib>Schaefer, C</creatorcontrib><creatorcontrib>Beck, M.I</creatorcontrib><title>Hydrophobicity, Solubility, and Emulsifying Properties of Enzyme-Modified Rice Endosperm Protein</title><title>Cereal chemistry</title><description>Rice endosperm protein was modified to enhance solubility and emulsifying properties by controlled enzymatic hydrolysis. The optimum degree of hydrolysis (DH) was determined for acid, neutral, and alkaline type proteases. Solubility and emulsifying properties of the hydrolysates were compared and correlated with DH and surface hydrophobicity. DH was positively associated with solubility of resulting protein hydrolysate regardless of the hydrolyzing enzyme, but enzyme specificity and DH interactively determined the emulsifying properties of the protein hydrolysate. The optimum DH was 6-10% for good emulsifying properties of rice protein, depending on enzyme specificity. High hydrophobic and sulfhydryl disulfide (SH-SS) interactions contributed to protein insolubility even at high DH. The exposure of buried hydrophobic regions of protein that accompanied high-temperature enzyme inactivation promoted aggregation and cross-linking of partially hydrolyzed proteins, thus decreasing the solubility and emulsifying properties of the resulting hydrolysate. Due to the highly insoluble nature of rice protein, surface hydrophobicity was not a reliable indicator for predicting protein solubility and emulsifying properties. Solubility and molecular flexibility are the essential factors in achieving good emulsifying properties of rice endosperm protein isolates.</description><subject>acid proteinases</subject><subject>alkaline proteinases</subject><subject>Biological and medical sciences</subject><subject>Cereal and baking product industries</subject><subject>chemical interactions</subject><subject>degree of hydrolysis</subject><subject>emulsifying properties</subject><subject>endosperm</subject><subject>enzymatic hydrolysis</subject><subject>enzyme activity</subject><subject>enzyme inactivation</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>hydrophobic interactions</subject><subject>hydrophobicity</subject><subject>neutral proteinases</subject><subject>protein aggregates</subject><subject>protein hydrolysates</subject><subject>protein-protein interactions</subject><subject>proteinases</subject><subject>rice</subject><subject>rice protein</subject><subject>solubility</subject><subject>sulfhydryl groups</subject><issn>0009-0352</issn><issn>1943-3638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkE1LAzEQhoMoWKtnjy6CN9cmm2w2OUqpVmhRrJ5jNh-asrupSYusv97UFjx6SmZ43meGAeAcwRsEORkp9WHanJGc5BATfAAGiBOcY4rZIRhACHnql8UxOIlxmUqMKjwAb9NeB7_68LVTbt1fZwvfbGrX_P5lp7NJu2mis73r3rOnRJqwdiZm3maT7rtvTT732llndPbslElN7WOC2i28Nq47BUdWNtGc7d8heL2bvIyn-ezx_mF8O8sVSdvmEktla4oIYhxbSyqukObY8BpXBWecMUIoorXVEpU1VVQXEpecqYLUUNMSD8HlzrsK_nNj4los_SZ0aaQoMISIYlolaLSDVPAxBmPFKrhWhl4gKLZXFOPxdDIXjAgitldMiau9VkYlGxtkp1z8izHOeVVszeWO-3KN6f_T_tZ7_8UuZ6UX8j0k9-uigCitzCDhvMQ_qceL8Q</recordid><startdate>200707</startdate><enddate>200707</enddate><creator>Paraman, I</creator><creator>Hettiarachchy, N.S</creator><creator>Schaefer, C</creator><creator>Beck, M.I</creator><general>The American Association of Cereal Chemists, Inc</general><general>American Association of Cereal Chemists</general><scope>FBQ</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>4T-</scope><scope>7X2</scope><scope>7XB</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FK</scope><scope>8G5</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>L6V</scope><scope>M0K</scope><scope>M2O</scope><scope>M7S</scope><scope>MBDVC</scope><scope>PATMY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>S0X</scope></search><sort><creationdate>200707</creationdate><title>Hydrophobicity, Solubility, and Emulsifying Properties of Enzyme-Modified Rice Endosperm Protein</title><author>Paraman, I ; Hettiarachchy, N.S ; Schaefer, C ; Beck, M.I</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4343-a3acfb6141893ff479c1d93e9b3729898844616bfda15b6c6d2a3598c24b0d653</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>acid proteinases</topic><topic>alkaline proteinases</topic><topic>Biological and medical sciences</topic><topic>Cereal and baking product industries</topic><topic>chemical interactions</topic><topic>degree of hydrolysis</topic><topic>emulsifying properties</topic><topic>endosperm</topic><topic>enzymatic hydrolysis</topic><topic>enzyme activity</topic><topic>enzyme inactivation</topic><topic>Food industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>hydrophobic interactions</topic><topic>hydrophobicity</topic><topic>neutral proteinases</topic><topic>protein aggregates</topic><topic>protein hydrolysates</topic><topic>protein-protein interactions</topic><topic>proteinases</topic><topic>rice</topic><topic>rice protein</topic><topic>solubility</topic><topic>sulfhydryl groups</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Paraman, I</creatorcontrib><creatorcontrib>Hettiarachchy, N.S</creatorcontrib><creatorcontrib>Schaefer, C</creatorcontrib><creatorcontrib>Beck, M.I</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Docstoc</collection><collection>Agricultural Science Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Engineering Collection</collection><collection>Agricultural Science Database</collection><collection>Research Library</collection><collection>Engineering Database</collection><collection>Research Library (Corporate)</collection><collection>Environmental Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Engineering Collection</collection><collection>Environmental Science Collection</collection><collection>ProQuest Central Basic</collection><collection>SIRS Editorial</collection><jtitle>Cereal chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Paraman, I</au><au>Hettiarachchy, N.S</au><au>Schaefer, C</au><au>Beck, M.I</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Hydrophobicity, Solubility, and Emulsifying Properties of Enzyme-Modified Rice Endosperm Protein</atitle><jtitle>Cereal chemistry</jtitle><date>2007-07</date><risdate>2007</risdate><volume>84</volume><issue>4</issue><spage>343</spage><epage>349</epage><pages>343-349</pages><issn>0009-0352</issn><eissn>1943-3638</eissn><coden>CECHAF</coden><abstract>Rice endosperm protein was modified to enhance solubility and emulsifying properties by controlled enzymatic hydrolysis. The optimum degree of hydrolysis (DH) was determined for acid, neutral, and alkaline type proteases. Solubility and emulsifying properties of the hydrolysates were compared and correlated with DH and surface hydrophobicity. DH was positively associated with solubility of resulting protein hydrolysate regardless of the hydrolyzing enzyme, but enzyme specificity and DH interactively determined the emulsifying properties of the protein hydrolysate. The optimum DH was 6-10% for good emulsifying properties of rice protein, depending on enzyme specificity. High hydrophobic and sulfhydryl disulfide (SH-SS) interactions contributed to protein insolubility even at high DH. The exposure of buried hydrophobic regions of protein that accompanied high-temperature enzyme inactivation promoted aggregation and cross-linking of partially hydrolyzed proteins, thus decreasing the solubility and emulsifying properties of the resulting hydrolysate. Due to the highly insoluble nature of rice protein, surface hydrophobicity was not a reliable indicator for predicting protein solubility and emulsifying properties. Solubility and molecular flexibility are the essential factors in achieving good emulsifying properties of rice endosperm protein isolates.</abstract><cop>St. Paul, MN</cop><pub>The American Association of Cereal Chemists, Inc</pub><doi>10.1094/cchem-84-4-0343</doi><tpages>7</tpages></addata></record> |
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| ispartof | Cereal chemistry, 2007-07, Vol.84 (4), p.343-349 |
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| source | Wiley Journals |
| subjects | acid proteinases alkaline proteinases Biological and medical sciences Cereal and baking product industries chemical interactions degree of hydrolysis emulsifying properties endosperm enzymatic hydrolysis enzyme activity enzyme inactivation Food industries Fundamental and applied biological sciences. Psychology hydrophobic interactions hydrophobicity neutral proteinases protein aggregates protein hydrolysates protein-protein interactions proteinases rice rice protein solubility sulfhydryl groups |
| title | Hydrophobicity, Solubility, and Emulsifying Properties of Enzyme-Modified Rice Endosperm Protein |
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