Combination of microwave heating and transglutaminase cross-linking enhances the stability of limonene emulsion carried by whey protein isolate

被引:16
作者
Bilawal, Akhunzada [1 ]
Wang, Xindi [1 ]
Oh, Kwang-Chol [1 ,2 ]
Qayum, Abdul [1 ]
Gantumur, Munkh-Amgalan [1 ]
Jiang, Zhanmei [1 ]
Hou, Juncai [1 ]
机构
[1] Northeast Agr Univ, Coll Food Sci, Key Lab Dairy Sci, Minist Educ, Harbin 150030, Peoples R China
[2] Pyongyang Technol Coll Food & Commod, Pyongyang, North Korea
关键词
Microwave; Whey protein isolates; D-limonene; Emulsion; Stability; MICROBIAL TRANSGLUTAMINASE; OXIDATIVE STABILITY; OPTIMIZATION; PERFORMANCE; EXTRACTION;
D O I
10.1016/j.fbio.2022.101684
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
In this study, we examined the effect of transglutaminase (TG) cross-linking time (0 h, 2 h, 4 h, 8 h, and 12 h) on the stability of limonene emulsion loaded by microwave-heated WPI (MWPI). Size exclusion chromatography results showed that molecular weight of TG-treated MWPI and WPI was enhanced with the increase in TG cross linking time (0-12 h). Microwave and TG cross-linking decreased particle size (7.55%) and increased zeta-potential (5.33%) and protein adsorption (4.58%) of WPI emulsion at TG cross-linking time of 12 h. CLSM results showed smaller droplet size of MWPI-TG emulsion and its uniform size. The obtained limonene emulsion loaded by MWPI-TG at 12 h showed the lowest creaming index and the strongest oxidative stability under aerobic conditions after 10thdays of storage. Thus, the combination of microwave heating and TG cross-linking effectively enhanced the stability of limonene emulsion stabilized by WPI and facilitating the application of WPI in the fields of food, medicine, cosmetics, and other areas.
引用
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页数:9
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