Effects of protein concentration, ionic strength, and heat treatment on the interfacial and emulsifying properties of coconut (Cocos nucifera L.) globulins
文献类型： 外文期刊
作者： Ma, Jingrong 1 ; Pan, Chuang 2 ; Chen, Haiming 1 ; Chen, Weijun 1 ; Pei, Jianfei 1 ; Zhang, Ming 1 ; Zhong, Qiuping 1 ; Chen, Wenxue 1 ; Zeng, Guangjin 3 ;
作者机构： 1.Hainan Univ, Coll Food Sci & Engn, HNU HSF Collaborat Innovat Lab, 58 People Rd, Haikou 570228, Peoples R China
2.Chinese Acad Fishery Sci, South China Sea Fisheries Res Inst, Natl R&D Ctr Aquat Prod Proc, Key Lab Aquat Prod Proc,Minist Agr & Rural Affairs, Guangzhou 510300, Peoples R China
3.Haikou Dongchang Pepper Co LTD, Haikou, Hainan, Peoples R China
关键词： Coconut globulins; Protein concentration; Ionic strength; Heat treatment; Interfacial properties; Emulsifying stability
期刊名称：FOOD CHEMISTRY-X （ 影响因子：6.1； 五年影响因子：6.4 ）
ISSN： 2590-1575
年卷期： 2023 年 20 卷
页码：
收录情况： SCI
摘要： This research aimed to investigate the effects of protein concentration (0.2 %-1.0 %), ionic strength (100-500 mM NaCl), and heat treatment (temperature: 80 and 90 degrees C; time: 15 and 30 min) on the interfacial and emul-sifying properties of coconut globulins (CG). When protein concentration was set at 0.2-0.6 %, the interfacial adsorption increased with the increasing of protein concentration. However, the lowest interfacial viscoelasticity was found when CG concentration was 0.6 %. When the protein concentration was higher than 0.6 %, the dilatational viscoelasticity increased with the increasing of protein concentration. The protein concentration showed positive effect on the emulsion stability of CG. The ionic strength showed positive effect on the interfacial adsorption but negative effects on the interfacial viscoelasticity and emulsion stability. Higher temperature and longer heating time brought worse interface behavior. The heated CG (90 degrees C, 30 min) had the worst interfacial behavior but the best emulsion stability.
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