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Inactivation of Soybean Bowman-Birk Inhibitor by Stevioside: Interaction Studies and Application to Soymilk.

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成果类型:
期刊论文
作者:
Liu, Chun;Luo, Lijuan;Wu, Ying;Yang, Xiaoquan;Dong, Jie;...
通讯作者:
Lin, Qinlu
作者机构:
[Dong, Jie; Luo, Feijun; Liu, Chun; Luo, Lijuan; Wu, Ying; Lin, Qinlu] Ctr South Univ Forestry & Technol, Sch Food Sci & Engn, Hunan Key Lab Proc Food Special Med Purpose, Natl Engn Lab Rice & Byprod Deep Proc, Changsha 410004, Hunan, Peoples R China.
[Yang, Xiaoquan] South China Univ Technol, Sch Food Sci & Engn, Res & Dev Ctr Food Prot, Guangzhou 510640, Guangdong, Peoples R China.
[Dong, Jie] Cent S Univ, Xiangya Sch Pharmaceut Sci, Changsha 410013, Hunan, Peoples R China.
[Zou, Yuan] South China Agr Univ, Sch Food Sci, Guangzhou 510642, Guangdong, Peoples R China.
[Shen, Yingbin] Jinan Univ, Sch Sci & Engn, Dept Food Sci & Engn, Guangzhou 510632, Guangdong, Peoples R China.
通讯机构:
[Lin, Qinlu] C
Ctr South Univ Forestry & Technol, Sch Food Sci & Engn, Hunan Key Lab Proc Food Special Med Purpose, Natl Engn Lab Rice & Byprod Deep Proc, Changsha 410004, Hunan, Peoples R China.
语种:
英文
关键词:
inactivation;interaction;soybean Bowman-Birk inhibitor;soymilk;stevioside
期刊:
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
ISSN:
0021-8561
年:
2019
卷:
67
期:
8
页码:
2255-2264
基金类别:
National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [31571874]; program for Science & Technology Innovation Talents of Hunan Province [2017TP1021 kc1704007]; Natural Science Foundation of Hunan ProvinceNatural Science Foundation of Hunan Province [2017JJ3528, 2018D2672]
机构署名:
本校为第一且通讯机构
院系归属:
食品科学与工程学院
摘要:
In this work, the interaction of the soybean Bowman-Birk inhibitor (BBI) with stevioside (STE) was studied by stopped-flow-fluorescence and molecular docking. STE's inactivation of protease-inhibitor activities in soymilk and the influence of STE addition on the sensory character of soymilk were also evaluated. The results indicate that STE binds BBI with a binding constant ( Ka) of 3.38 x 10(5) L mol(-1) to form a 1:1 complex. The docking study reveals that two hydrogen bonds are formed between the side-chain of Lys16 (reactive site 1) of BBI and the glucose-ring hydroxyl groups of STE, which...

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