Effect of sorbed water on the thermal stability of soybean [Glycine max] protein
A soybean protein isolate (SPI), and its beta-conglycinin and glycinin componets were obtained from defatted soybean flour by applying dissolution and precipitation based on the difference in their solubility depending on each isoelectric point. The purity evaluated by SDS- PAGE of the beta-conglyci...
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| Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2006-09, Vol.70 (9), p.2096-2103 |
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| creator | Tsukada, H.(Tokyo Univ. of Agriculture and Technology, Fuchu (Japan). Faculty of Agriculture) Takano, K Hattori, M Yoshida, T Kanuma, S Takahashi, K |
| description | A soybean protein isolate (SPI), and its beta-conglycinin and glycinin componets were obtained from defatted soybean flour by applying dissolution and precipitation based on the difference in their solubility depending on each isoelectric point. The purity evaluated by SDS- PAGE of the beta-conglycinin and glycinin preparations was about 84% and 80%, respectively, resulting in a clear difference in the pH dependence on solubility. A BET plot derived from the water sorption isotherm at 25 deg C showed that the amount of the monolayer adsorption of these preparations was about 6-9%, the value for the beta-conglycinin preparation being about 1.5 times higher than that for the glycinin preparation. The beta-conglycinin and glycinin preparations were respectively denatured at around 75 deg C and 86 deg C in the presence of excess water, whereas the denaturation temperature of both preparations was markedly increased by decreasing sorbed water content below 40%, corresponding well with the unfrozen water content. |
| doi_str_mv | 10.1271/bbb.60041 |
| format | Article |
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Faculty of Agriculture) ; Takano, K ; Hattori, M ; Yoshida, T ; Kanuma, S ; Takahashi, K</creator><creatorcontrib>Tsukada, H.(Tokyo Univ. of Agriculture and Technology, Fuchu (Japan). Faculty of Agriculture) ; Takano, K ; Hattori, M ; Yoshida, T ; Kanuma, S ; Takahashi, K</creatorcontrib><description>A soybean protein isolate (SPI), and its beta-conglycinin and glycinin componets were obtained from defatted soybean flour by applying dissolution and precipitation based on the difference in their solubility depending on each isoelectric point. The purity evaluated by SDS- PAGE of the beta-conglycinin and glycinin preparations was about 84% and 80%, respectively, resulting in a clear difference in the pH dependence on solubility. A BET plot derived from the water sorption isotherm at 25 deg C showed that the amount of the monolayer adsorption of these preparations was about 6-9%, the value for the beta-conglycinin preparation being about 1.5 times higher than that for the glycinin preparation. The beta-conglycinin and glycinin preparations were respectively denatured at around 75 deg C and 86 deg C in the presence of excess water, whereas the denaturation temperature of both preparations was markedly increased by decreasing sorbed water content below 40%, corresponding well with the unfrozen water content.</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1271/bbb.60041</identifier><identifier>PMID: 16960389</identifier><language>eng</language><publisher>Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry</publisher><subject>Adsorption ; ANALISIS TERMICO ; ANALYSE THERMIQUE ; Antigens, Plant ; Biological and medical sciences ; Calorimetry, Differential Scanning ; CONTENIDO DE HUMEDAD ; DENATURATION ; DESNATURALIZACION ; differential scanning calorimetry ; Drug Stability ; Electrophoresis, Polyacrylamide Gel ; Fundamental and applied biological sciences. Psychology ; Globulins - chemistry ; HEAT TOLERANCE ; Hot Temperature ; Hydrogen-Ion Concentration ; Isoelectric Point ; MOISTURE CONTENT ; Protein Denaturation ; PROTEINAS DE RESERVA ; PROTEINE DE RESERVE ; Seed Storage Proteins ; SOJA ; SORCION ; SORPTION ; soybean protein isolate ; Soybean Proteins - chemistry ; SOYBEANS ; STORAGE PROTEINS ; TENEUR EN EAU ; THERMAL ANALYSIS ; thermal stability ; TOLERANCE A LA CHALEUR ; TOLERANCIA AL CALOR ; unfrozen water ; Water - chemistry ; water sorption isotherm</subject><ispartof>Bioscience, biotechnology, and biochemistry, 2006-09, Vol.70 (9), p.2096-2103</ispartof><rights>2006 by Japan Society for Bioscience, Biotechnology, and Agrochemistry 2006</rights><rights>2007 INIST-CNRS</rights><rights>Copyright Japan Science and Technology Agency 2006</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c635t-b248b766543a3c5984189f262d019e35ad15f973a4952d31f1ee2c6c4d3859ae3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18346000$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16960389$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tsukada, H.(Tokyo Univ. of Agriculture and Technology, Fuchu (Japan). Faculty of Agriculture)</creatorcontrib><creatorcontrib>Takano, K</creatorcontrib><creatorcontrib>Hattori, M</creatorcontrib><creatorcontrib>Yoshida, T</creatorcontrib><creatorcontrib>Kanuma, S</creatorcontrib><creatorcontrib>Takahashi, K</creatorcontrib><title>Effect of sorbed water on the thermal stability of soybean [Glycine max] protein</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>A soybean protein isolate (SPI), and its beta-conglycinin and glycinin componets were obtained from defatted soybean flour by applying dissolution and precipitation based on the difference in their solubility depending on each isoelectric point. The purity evaluated by SDS- PAGE of the beta-conglycinin and glycinin preparations was about 84% and 80%, respectively, resulting in a clear difference in the pH dependence on solubility. A BET plot derived from the water sorption isotherm at 25 deg C showed that the amount of the monolayer adsorption of these preparations was about 6-9%, the value for the beta-conglycinin preparation being about 1.5 times higher than that for the glycinin preparation. The beta-conglycinin and glycinin preparations were respectively denatured at around 75 deg C and 86 deg C in the presence of excess water, whereas the denaturation temperature of both preparations was markedly increased by decreasing sorbed water content below 40%, corresponding well with the unfrozen water content.</description><subject>Adsorption</subject><subject>ANALISIS TERMICO</subject><subject>ANALYSE THERMIQUE</subject><subject>Antigens, Plant</subject><subject>Biological and medical sciences</subject><subject>Calorimetry, Differential Scanning</subject><subject>CONTENIDO DE HUMEDAD</subject><subject>DENATURATION</subject><subject>DESNATURALIZACION</subject><subject>differential scanning calorimetry</subject><subject>Drug Stability</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Globulins - chemistry</subject><subject>HEAT TOLERANCE</subject><subject>Hot Temperature</subject><subject>Hydrogen-Ion Concentration</subject><subject>Isoelectric Point</subject><subject>MOISTURE CONTENT</subject><subject>Protein Denaturation</subject><subject>PROTEINAS DE RESERVA</subject><subject>PROTEINE DE RESERVE</subject><subject>Seed Storage Proteins</subject><subject>SOJA</subject><subject>SORCION</subject><subject>SORPTION</subject><subject>soybean protein isolate</subject><subject>Soybean Proteins - chemistry</subject><subject>SOYBEANS</subject><subject>STORAGE PROTEINS</subject><subject>TENEUR EN EAU</subject><subject>THERMAL ANALYSIS</subject><subject>thermal stability</subject><subject>TOLERANCE A LA CHALEUR</subject><subject>TOLERANCIA AL CALOR</subject><subject>unfrozen water</subject><subject>Water - chemistry</subject><subject>water sorption isotherm</subject><issn>0916-8451</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpt0E1rFTEUBuAgir1WF_4AJSAKLqbm-2MppValYBe6EglJJtEpmUlNcqnz702dKwVxEQLhOe8JLwBPMTrBROI3zrkTgRDD98AOUyYHoZm8D3ZIYzEoxvEReFTrFUL9geOH4AgLLRBVegcuz2IMvsEcYc3FhRHe2BYKzAtsP8LtKbNNsDbrpjS1dYOrC3aBX8_T6qclwNn--gavS25hWh6DB9GmGp4c7mPw5d3Z59P3w8Wn8w-nby8GLyhvgyNMOSkEZ9RSz7ViWOlIBBkR1oFyO2IetaSWaU5GiiMOgXjh2UgV1zbQY_Bqy-17f-5DbWaeqg8p2SXkfTVCKa2lIh2--Ade5X1Z-t8MZkwrzCUVXb3elC-51hKiuS7TbMtqMDK3JZtesvlTcrfPD4l7N4fxTh5a7eDlAdjqbYrFLn6qd05R1pNQd2xz0xJz7_kmlzSaZteUy98h-r_9z7axaLOx30tXHy8JQrJHSkbob7djnPM</recordid><startdate>20060901</startdate><enddate>20060901</enddate><creator>Tsukada, H.(Tokyo Univ. of Agriculture and Technology, Fuchu (Japan). Faculty of Agriculture)</creator><creator>Takano, K</creator><creator>Hattori, M</creator><creator>Yoshida, T</creator><creator>Kanuma, S</creator><creator>Takahashi, K</creator><general>Japan Society for Bioscience, Biotechnology, and Agrochemistry</general><general>Japan Society for Bioscience Biotechnology and Agrochemistry</general><general>Oxford University Press</general><scope>FBQ</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>7X8</scope></search><sort><creationdate>20060901</creationdate><title>Effect of sorbed water on the thermal stability of soybean [Glycine max] protein</title><author>Tsukada, H.(Tokyo Univ. of Agriculture and Technology, Fuchu (Japan). Faculty of Agriculture) ; Takano, K ; Hattori, M ; Yoshida, T ; Kanuma, S ; Takahashi, K</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c635t-b248b766543a3c5984189f262d019e35ad15f973a4952d31f1ee2c6c4d3859ae3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Adsorption</topic><topic>ANALISIS TERMICO</topic><topic>ANALYSE THERMIQUE</topic><topic>Antigens, Plant</topic><topic>Biological and medical sciences</topic><topic>Calorimetry, Differential Scanning</topic><topic>CONTENIDO DE HUMEDAD</topic><topic>DENATURATION</topic><topic>DESNATURALIZACION</topic><topic>differential scanning calorimetry</topic><topic>Drug Stability</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Globulins - chemistry</topic><topic>HEAT TOLERANCE</topic><topic>Hot Temperature</topic><topic>Hydrogen-Ion Concentration</topic><topic>Isoelectric Point</topic><topic>MOISTURE CONTENT</topic><topic>Protein Denaturation</topic><topic>PROTEINAS DE RESERVA</topic><topic>PROTEINE DE RESERVE</topic><topic>Seed Storage Proteins</topic><topic>SOJA</topic><topic>SORCION</topic><topic>SORPTION</topic><topic>soybean protein isolate</topic><topic>Soybean Proteins - chemistry</topic><topic>SOYBEANS</topic><topic>STORAGE PROTEINS</topic><topic>TENEUR EN EAU</topic><topic>THERMAL ANALYSIS</topic><topic>thermal stability</topic><topic>TOLERANCE A LA CHALEUR</topic><topic>TOLERANCIA AL CALOR</topic><topic>unfrozen water</topic><topic>Water - chemistry</topic><topic>water sorption isotherm</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tsukada, H.(Tokyo Univ. of Agriculture and Technology, Fuchu (Japan). Faculty of Agriculture)</creatorcontrib><creatorcontrib>Takano, K</creatorcontrib><creatorcontrib>Hattori, M</creatorcontrib><creatorcontrib>Yoshida, T</creatorcontrib><creatorcontrib>Kanuma, S</creatorcontrib><creatorcontrib>Takahashi, K</creatorcontrib><collection>AGRIS</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>MEDLINE - Academic</collection><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tsukada, H.(Tokyo Univ. of Agriculture and Technology, Fuchu (Japan). Faculty of Agriculture)</au><au>Takano, K</au><au>Hattori, M</au><au>Yoshida, T</au><au>Kanuma, S</au><au>Takahashi, K</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effect of sorbed water on the thermal stability of soybean [Glycine max] protein</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><addtitle>Biosci Biotechnol Biochem</addtitle><date>2006-09-01</date><risdate>2006</risdate><volume>70</volume><issue>9</issue><spage>2096</spage><epage>2103</epage><pages>2096-2103</pages><issn>0916-8451</issn><eissn>1347-6947</eissn><abstract>A soybean protein isolate (SPI), and its beta-conglycinin and glycinin componets were obtained from defatted soybean flour by applying dissolution and precipitation based on the difference in their solubility depending on each isoelectric point. The purity evaluated by SDS- PAGE of the beta-conglycinin and glycinin preparations was about 84% and 80%, respectively, resulting in a clear difference in the pH dependence on solubility. A BET plot derived from the water sorption isotherm at 25 deg C showed that the amount of the monolayer adsorption of these preparations was about 6-9%, the value for the beta-conglycinin preparation being about 1.5 times higher than that for the glycinin preparation. The beta-conglycinin and glycinin preparations were respectively denatured at around 75 deg C and 86 deg C in the presence of excess water, whereas the denaturation temperature of both preparations was markedly increased by decreasing sorbed water content below 40%, corresponding well with the unfrozen water content.</abstract><cop>Tokyo</cop><pub>Japan Society for Bioscience, Biotechnology, and Agrochemistry</pub><pmid>16960389</pmid><doi>10.1271/bbb.60041</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Bioscience, biotechnology, and biochemistry, 2006-09, Vol.70 (9), p.2096-2103 |
| issn | 0916-8451 1347-6947 |
| language | eng |
| recordid | cdi_proquest_journals_1449815736 |
| source | MEDLINE; Oxford University Press Journals All Titles (1996-Current); J-STAGE (Japan Science & Technology Information Aggregator, Electronic) Freely Available Titles - Japanese; Open Access Titles of Japan; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | Adsorption ANALISIS TERMICO ANALYSE THERMIQUE Antigens, Plant Biological and medical sciences Calorimetry, Differential Scanning CONTENIDO DE HUMEDAD DENATURATION DESNATURALIZACION differential scanning calorimetry Drug Stability Electrophoresis, Polyacrylamide Gel Fundamental and applied biological sciences. Psychology Globulins - chemistry HEAT TOLERANCE Hot Temperature Hydrogen-Ion Concentration Isoelectric Point MOISTURE CONTENT Protein Denaturation PROTEINAS DE RESERVA PROTEINE DE RESERVE Seed Storage Proteins SOJA SORCION SORPTION soybean protein isolate Soybean Proteins - chemistry SOYBEANS STORAGE PROTEINS TENEUR EN EAU THERMAL ANALYSIS thermal stability TOLERANCE A LA CHALEUR TOLERANCIA AL CALOR unfrozen water Water - chemistry water sorption isotherm |
| title | Effect of sorbed water on the thermal stability of soybean [Glycine max] protein |
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