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Influence of substrate aggregation state on the enzymatic-induced crosslinking of soy protein isolate

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成果类型:
期刊论文
作者:
Wang, Xufeng*;Wang, Yuqi;Wang, Xiongshi;Xing, Yunhao;Kuang, Chuyu;...
通讯作者:
Wang, Xufeng;Cheng, YH;Wang, SY
作者机构:
[Cheng, Yunhui; Wang, Xufeng; Xing, Yunhao; Cheng, YH; Wang, Xiongshi] Changsha Univ Sci & Technol, Sch Food Sci & Bioengn, Changsha, Hunan, Peoples R China.
[Wang, Shaoyun; Wang, Yuqi; Wang, SY] Fuzhou Univ, Coll Biol Sci & Engn, Fuzhou, Fujian, Peoples R China.
[Luo, Kaiyun; Kuang, Chuyu] Hunan Agr Univ, Coll Food Sci & Technol, Changsha, Hunan, Peoples R China.
通讯机构:
[Wang, XF; Cheng, YH ] C
[Wang, SY ] F
Changsha Univ Sci & Technol, Sch Food Sci & Bioengn, Changsha, Hunan, Peoples R China.
Fuzhou Univ, Coll Biol Sci & Engn, Fuzhou, Fujian, Peoples R China.
语种:
英文
关键词:
Aggregation;Crosslinking;Gel;Soy protein isolate;Transglutaminase
期刊:
Food Chemistry
ISSN:
0308-8146
年:
2024
卷:
442
页码:
138484
基金类别:
Program of National Natural Science Foundation of China (NSFC) [32101986]; Natural Science Foundation of Fujian Province, China [2020J05128]
机构署名:
本校为其他机构
院系归属:
食品科学技术学院
摘要:
Transglutaminase (TGase) induced-crosslinking of soy protein isolate (SPI) was markedly influenced by the substrate aggregation state. Results showed that appropriate heating significantly accelerated the TGase crosslinking, and the 7S and 11S acidic subunits were more susceptible to the enzyme than the 11S basic proteins. The content of epsilon-(gamma-glutamyl)-lysine isopeptide bonds increased from 4.74 to 8.61 mu mol/g protein when the heating intensity was increased from 75 degree celsius for 15 min to 95 degree celsius for 30 min, due to sufficient unfolding of the protein structure. Rheo...

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