详细信息

Physicochemical Characteristics of Edible Bird's Nest Proteins and Their Cooking Processing Properties  ( SCI-EXPANDED收录 EI收录)  

文献类型:期刊文献

英文题名:Physicochemical Characteristics of Edible Bird's Nest Proteins and Their Cooking Processing Properties

作者:Huang, Sha[1,2];Zhao, Liming[1,3];Chen, Qiming[1,3];Qin, Zhen[1,3];Zhou, Jiachun[1,3];Qiu, Yongjun[1,3];Zhang, Yin[4];Ma, Mingyue[5]

机构:[1]East China Univ Sci & Technol, Sch Biotechnol, R&D Ctr Separat & Extract Technol Fermentat Ind, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[2]Lishui Acad Agr Sci, Lishui 323000, Zhejiang, Peoples R China;[3]SCICBT, Shanghai 200237, Peoples R China;[4]Chengdu Univ, Key Lab Meat Proc Sichuan, Chengdu 610106, Sichuan, Peoples R China;[5]Chongqing Univ Posts & Telecommun, Sch Bioinformat, Chongqing 400065, Peoples R China

年份:2018

卷号:14

期号:3

外文期刊名:INTERNATIONAL JOURNAL OF FOOD ENGINEERING

收录:;EI(收录号:20181705058361);WOS:【SCI-EXPANDED(收录号:WOS:000431384400005)】;

基金:The authors would like to thank the National Natural Science Foundation of China (31371725), the National High Technology Research, Development Program of China (863 Program) (2014AA021202), Fundamental Research Funds for the Central Universities (222201717026), Scientific Research Foundation of Chongqing University of Posts and Telecommunications(A2016-87) and Chongqing Education Commission Research Project (KJ1704094) for their financial support.

语种:英文

外文关键词:edible bird's nest proteins; extraction method; physicochemical and processing properties; water-holding capacity

摘要:Edible bird's nest (EBN) has a high nutritional and medicinal value. In this study, physicochemical and processing properties of EBN proteins were investigated for better application of EBN. EBN proteins were extracted by combination of several methods. Electrophoresis showed that EBN contained proteins with molecular weight of 128, 106, 80, 55, 43, and 34 kDa. The denaturation temperature of EBN proteins was 62.5 degrees C and heating promoted hydrophobicity as well as dramatically affecting the gel microstructure of EBN proteins. EBN proteins also showed excellent emulsifying activity and stability while their foaming properties were not good enough.

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