Please use this identifier to cite or link to this item:
http://hdl.handle.net/10397/63755
DC Field | Value | Language |
---|---|---|
dc.contributor | Department of Applied Biology and Chemical Technology | - |
dc.creator | Huang, HH | - |
dc.creator | Kwok, KC | - |
dc.creator | Liang, HH | - |
dc.creator | Gao, KR | - |
dc.date.accessioned | 2017-02-09T08:30:31Z | - |
dc.date.available | 2017-02-09T08:30:31Z | - |
dc.identifier.issn | 0512-7955 | - |
dc.identifier.uri | http://hdl.handle.net/10397/63755 | - |
dc.language.iso | zh | en_US |
dc.publisher | 中國學術期刊(光盤版)電子雜誌社 | en_US |
dc.rights | © 2001 中国学术期刊电子杂志出版社。本内容的使用仅限于教育、科研之目的。 | en_US |
dc.rights | © 2001 China Academic Journal Electronic Publishing House. It is to be used strictly for educational and research purposes. | en_US |
dc.subject | Soymilk | en_US |
dc.subject | Thermal treatment | en_US |
dc.subject | SDS PAGE | en_US |
dc.subject | Trypsin inhibitor | en_US |
dc.subject | Sulfhydryl bond | en_US |
dc.title | Changes of SDS-PAGE patterns of soymilk protein and trypsin inhibitor activity induced by heating | en_US |
dc.type | Journal/Magazine Article | en_US |
dc.identifier.spage | 140 | - |
dc.identifier.epage | 144 | - |
dc.identifier.volume | 23 | - |
dc.identifier.issue | 2 | - |
dcterms.abstract | Objective: To evaluate the heating effects on SDS PAGE patterns of soymilk protein, trypsin inhibitor activity and sulfhydryl bond content in soymilkMethods: Soymilk samples were heated at 95 ℃,120 ℃ and 140 ℃.SDS PAGE was adopted to detect the pattern changes of soymilk proteins after heating and β mercaptoethanol pretreatment. Trypsin activities were analyzed to detect the changes of trypsin inhibitor activities. Ellman method was used to detect sulfhydryl bond.Results: The protein bands of 7,8,11,12,13,14,15,16 disappeared and one new band(band 17)with Mr of 104 620 appeared in the SDS PAGE pattern of soymilk proteins after heated at 95 ℃,120 ℃ and 140 ℃. The sulfhydryl bond content decreased after heating and this change contributed to the pattern change of soymilk protein by β mercaptoethanol pretreatment and by determining the sulfhydryl bond content. The holding time to inactivate 90% of soy bean inhibitor activity at 95 ℃ ,120 ℃ and 140 ℃ were 35 min, 7 min and 60 s respectively.Conclusion: Heating treatment may change the sulfhydryl bond and SDS PAGE pattern of soymilk proteins. The TDT curve indicates that the holding time required to inactivate 90% of soybean trypsin inhibitor could be reduced ten folds by raising 30 ℃ within the temperature range of 95 140 ℃. | - |
dcterms.accessRights | open access | en_US |
dcterms.alternative | 豆奶蛋白組分和胰蛋白酶抑制劑活性的熱變化 | - |
dcterms.bibliographicCitation | 營養學報 (Acta nutrimenta sinica), 2001, v. 23, no. 2, p. 140-144 | - |
dcterms.isPartOf | 營養學報 (Acta nutrimenta sinica) | - |
dcterms.issued | 2001 | - |
dc.identifier.rosgroupid | r08501 | - |
dc.description.ros | 2001-2002 > Academic research: refereed > Publication in refereed journal | - |
dc.description.oa | Version of Record | en_US |
dc.identifier.FolderNumber | OA_IR/PIRA | en_US |
dc.description.pubStatus | Published | en_US |
Appears in Collections: | Journal/Magazine Article |
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File | Description | Size | Format | |
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r08501.pdf | 195.57 kB | Adobe PDF | View/Open |
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