Functional Properties of Oat Globulin Modified by a Calcium-Independent Microbial Transglutaminase
Oat globulin was modified by a calcium-independent microbial transglutaminase (TG). The TG-polymerized protein had higher solubility than the control at acidic pH and had improved water- and fat-binding properties. Incubation of 10% (w/v) oat globulin dispersions in the presence of TG at 37 °C led t...
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| Veröffentlicht in: | Journal of agricultural and food chemistry 2002-04, Vol.50 (9), p.2666-2672 |
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| creator | Siu, Nai-Chi Ma, Ching-Yung Mock, Wai-Yin Mine, Yoshinori |
| description | Oat globulin was modified by a calcium-independent microbial transglutaminase (TG). The TG-polymerized protein had higher solubility than the control at acidic pH and had improved water- and fat-binding properties. Incubation of 10% (w/v) oat globulin dispersions in the presence of TG at 37 °C led to the formation of a well-developed viscoelastic gel network with a microstructure characterized by thick strands and large clusters. The TG-induced gels had higher modulus values, lower loss tangent values, and lower frequency dependency than the heat-induced gels. The TG-induced gel system has the characteristics of classical polymer gel with permanent “chemical” cross-links, whereas the heat-denatured system has the characteristics of a temporary “physical” gel with breakable cross-links. Fourier transform infrared spectroscopy showed marked shift and intensity changes in several major bands, suggesting pronounced changes in protein conformation during TG-induced gelation. Aggregation of protein molecules was also indicated by the progressive increases in two infrared bands (1679−1682 and 1622−1625 cm-1) associated with the formation of intermolecular β-sheets and strands. Results suggest that new food polymers with unique functionality can be produced from oat globulin treated with TG and that elastic gels can be formed near neutral pH, instead of the alkaline pH required for thermally induced oat globulin gels. Keywords: Transglutaminase; oat globulin; functional properties; gelation, rheology |
| doi_str_mv | 10.1021/jf011163p |
| format | Article |
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The TG-polymerized protein had higher solubility than the control at acidic pH and had improved water- and fat-binding properties. Incubation of 10% (w/v) oat globulin dispersions in the presence of TG at 37 °C led to the formation of a well-developed viscoelastic gel network with a microstructure characterized by thick strands and large clusters. The TG-induced gels had higher modulus values, lower loss tangent values, and lower frequency dependency than the heat-induced gels. The TG-induced gel system has the characteristics of classical polymer gel with permanent “chemical” cross-links, whereas the heat-denatured system has the characteristics of a temporary “physical” gel with breakable cross-links. Fourier transform infrared spectroscopy showed marked shift and intensity changes in several major bands, suggesting pronounced changes in protein conformation during TG-induced gelation. Aggregation of protein molecules was also indicated by the progressive increases in two infrared bands (1679−1682 and 1622−1625 cm-1) associated with the formation of intermolecular β-sheets and strands. Results suggest that new food polymers with unique functionality can be produced from oat globulin treated with TG and that elastic gels can be formed near neutral pH, instead of the alkaline pH required for thermally induced oat globulin gels. Keywords: Transglutaminase; oat globulin; functional properties; gelation, rheology</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/jf011163p</identifier><identifier>PMID: 11958639</identifier><identifier>CODEN: JAFCAU</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts ; Avena - chemistry ; Biological and medical sciences ; Calcium - pharmacology ; Elasticity ; Food industries ; Fundamental and applied biological sciences. Psychology ; Gels - chemistry ; Gels - metabolism ; Hot Temperature ; Hydrogen-Ion Concentration ; Plant Proteins - chemistry ; Plant Proteins - metabolism ; Plant Proteins - physiology ; Polymers - metabolism ; Rheology ; Seeds - chemistry ; Solubility ; Spectroscopy, Fourier Transform Infrared ; Temperature ; Transglutaminases - metabolism ; Viscosity</subject><ispartof>Journal of agricultural and food chemistry, 2002-04, Vol.50 (9), p.2666-2672</ispartof><rights>Copyright © 2002 American Chemical Society</rights><rights>2002 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a410t-4f3d213881d9e62eba8b92a088a5cfafc68039c03ccc00e37c30e1c6671ace963</citedby><cites>FETCH-LOGICAL-a410t-4f3d213881d9e62eba8b92a088a5cfafc68039c03ccc00e37c30e1c6671ace963</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/jf011163p$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jf011163p$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=13619451$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11958639$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Siu, Nai-Chi</creatorcontrib><creatorcontrib>Ma, Ching-Yung</creatorcontrib><creatorcontrib>Mock, Wai-Yin</creatorcontrib><creatorcontrib>Mine, Yoshinori</creatorcontrib><title>Functional Properties of Oat Globulin Modified by a Calcium-Independent Microbial Transglutaminase</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>Oat globulin was modified by a calcium-independent microbial transglutaminase (TG). The TG-polymerized protein had higher solubility than the control at acidic pH and had improved water- and fat-binding properties. Incubation of 10% (w/v) oat globulin dispersions in the presence of TG at 37 °C led to the formation of a well-developed viscoelastic gel network with a microstructure characterized by thick strands and large clusters. The TG-induced gels had higher modulus values, lower loss tangent values, and lower frequency dependency than the heat-induced gels. The TG-induced gel system has the characteristics of classical polymer gel with permanent “chemical” cross-links, whereas the heat-denatured system has the characteristics of a temporary “physical” gel with breakable cross-links. Fourier transform infrared spectroscopy showed marked shift and intensity changes in several major bands, suggesting pronounced changes in protein conformation during TG-induced gelation. Aggregation of protein molecules was also indicated by the progressive increases in two infrared bands (1679−1682 and 1622−1625 cm-1) associated with the formation of intermolecular β-sheets and strands. Results suggest that new food polymers with unique functionality can be produced from oat globulin treated with TG and that elastic gels can be formed near neutral pH, instead of the alkaline pH required for thermally induced oat globulin gels. Keywords: Transglutaminase; oat globulin; functional properties; gelation, rheology</description><subject>Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts</subject><subject>Avena - chemistry</subject><subject>Biological and medical sciences</subject><subject>Calcium - pharmacology</subject><subject>Elasticity</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gels - chemistry</subject><subject>Gels - metabolism</subject><subject>Hot Temperature</subject><subject>Hydrogen-Ion Concentration</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - metabolism</subject><subject>Plant Proteins - physiology</subject><subject>Polymers - metabolism</subject><subject>Rheology</subject><subject>Seeds - chemistry</subject><subject>Solubility</subject><subject>Spectroscopy, Fourier Transform Infrared</subject><subject>Temperature</subject><subject>Transglutaminases - metabolism</subject><subject>Viscosity</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0UFv0zAUB3ALMbGyceALoFxA4hDmFzeOfUSFlUmrVmkdHK0Xx0YuTpzZicS-PUat1gsSF_vwfvrr-W9C3gL9BLSCq72lAMDZ-IIsoK5oWQOIl2RB87AUNYdz8jqlPaVU1A19Rc4BZC04kwvSXs-DnlwY0BfbGEYTJ2dSEWxxh1Ox9qGdvRuKTeicdaYr2qcCixV67ea-vBk6M5p8DFOxcTqG1uWYXcQh_fTzhL0bMJlLcmbRJ_PmeF-Qh-uvu9W38vZufbP6fFviEuhULi3rKmBCQCcNr0yLopUVUiGw1hat5oIyqSnTWlNqWKMZNaA5bwC1kZxdkA-H3DGGx9mkSfUuaeM9DibMSTXAQXJZ_ReC4DKvITP8eID5aSlFY9UYXY_xSQFVf5tXz81n--4YOre96U7yWHUG748Ak0Zvc0vapZNjebtlDdmVB-fSZH4_zzH-UrxhTa1223t1D1u6-fLju1qfclEntQ9zzF-Z_rHgH72bpss</recordid><startdate>20020424</startdate><enddate>20020424</enddate><creator>Siu, Nai-Chi</creator><creator>Ma, Ching-Yung</creator><creator>Mock, Wai-Yin</creator><creator>Mine, Yoshinori</creator><general>American Chemical Society</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>AAYXX</scope><scope>CITATION</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20020424</creationdate><title>Functional Properties of Oat Globulin Modified by a Calcium-Independent Microbial Transglutaminase</title><author>Siu, Nai-Chi ; Ma, Ching-Yung ; Mock, Wai-Yin ; Mine, Yoshinori</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a410t-4f3d213881d9e62eba8b92a088a5cfafc68039c03ccc00e37c30e1c6671ace963</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts</topic><topic>Avena - chemistry</topic><topic>Biological and medical sciences</topic><topic>Calcium - pharmacology</topic><topic>Elasticity</topic><topic>Food industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gels - chemistry</topic><topic>Gels - metabolism</topic><topic>Hot Temperature</topic><topic>Hydrogen-Ion Concentration</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - metabolism</topic><topic>Plant Proteins - physiology</topic><topic>Polymers - metabolism</topic><topic>Rheology</topic><topic>Seeds - chemistry</topic><topic>Solubility</topic><topic>Spectroscopy, Fourier Transform Infrared</topic><topic>Temperature</topic><topic>Transglutaminases - metabolism</topic><topic>Viscosity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Siu, Nai-Chi</creatorcontrib><creatorcontrib>Ma, Ching-Yung</creatorcontrib><creatorcontrib>Mock, Wai-Yin</creatorcontrib><creatorcontrib>Mine, Yoshinori</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>CrossRef</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Siu, Nai-Chi</au><au>Ma, Ching-Yung</au><au>Mock, Wai-Yin</au><au>Mine, Yoshinori</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Functional Properties of Oat Globulin Modified by a Calcium-Independent Microbial Transglutaminase</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>2002-04-24</date><risdate>2002</risdate><volume>50</volume><issue>9</issue><spage>2666</spage><epage>2672</epage><pages>2666-2672</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>Oat globulin was modified by a calcium-independent microbial transglutaminase (TG). The TG-polymerized protein had higher solubility than the control at acidic pH and had improved water- and fat-binding properties. Incubation of 10% (w/v) oat globulin dispersions in the presence of TG at 37 °C led to the formation of a well-developed viscoelastic gel network with a microstructure characterized by thick strands and large clusters. The TG-induced gels had higher modulus values, lower loss tangent values, and lower frequency dependency than the heat-induced gels. The TG-induced gel system has the characteristics of classical polymer gel with permanent “chemical” cross-links, whereas the heat-denatured system has the characteristics of a temporary “physical” gel with breakable cross-links. Fourier transform infrared spectroscopy showed marked shift and intensity changes in several major bands, suggesting pronounced changes in protein conformation during TG-induced gelation. Aggregation of protein molecules was also indicated by the progressive increases in two infrared bands (1679−1682 and 1622−1625 cm-1) associated with the formation of intermolecular β-sheets and strands. Results suggest that new food polymers with unique functionality can be produced from oat globulin treated with TG and that elastic gels can be formed near neutral pH, instead of the alkaline pH required for thermally induced oat globulin gels. Keywords: Transglutaminase; oat globulin; functional properties; gelation, rheology</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>11958639</pmid><doi>10.1021/jf011163p</doi><tpages>7</tpages></addata></record> |
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| subjects | Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts Avena - chemistry Biological and medical sciences Calcium - pharmacology Elasticity Food industries Fundamental and applied biological sciences. Psychology Gels - chemistry Gels - metabolism Hot Temperature Hydrogen-Ion Concentration Plant Proteins - chemistry Plant Proteins - metabolism Plant Proteins - physiology Polymers - metabolism Rheology Seeds - chemistry Solubility Spectroscopy, Fourier Transform Infrared Temperature Transglutaminases - metabolism Viscosity |
| title | Functional Properties of Oat Globulin Modified by a Calcium-Independent Microbial Transglutaminase |
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