Please use this identifier to cite or link to this item: http://hdl.handle.net/10397/63755
Title: Changes of SDS-PAGE patterns of soymilk protein and trypsin inhibitor activity induced by heating
Other Titles: 豆奶蛋白組分和胰蛋白酶抑制劑活性的熱變化
Authors: Huang, HH
Kwok, KC
Liang, HH 
Gao, KR
Keywords: Soymilk
Thermal treatment
SDS PAGE
Trypsin inhibitor
Sulfhydryl bond
Issue Date: 2001
Publisher: 中國學術期刊(光盤版)電子雜誌社
Source: 營養學報 (Acta nutrimenta sinica), 2001, v. 23, no. 2, p. 140-144 How to cite?
Journal: 營養學報 (Acta nutrimenta sinica) 
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 ℃.
URI: http://hdl.handle.net/10397/63755
ISSN: 0512-7955
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。
© 2001 China Academic Journal Electronic Publishing House. It is to be used strictly for educational and research purposes.
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