Consequences of superfine grinding treatment on structure, physicochemical and rheological properties of transglutaminase-crosslinked whey protein isolate

被引:67
作者
Wang, Chunyan [1 ]
Li, Tianqi [1 ]
Ma, Ling [1 ]
Li, Tong [1 ]
Yu, Haiying [1 ]
Hou, Juncai [1 ]
Jiang, Zhanmei [1 ]
机构
[1] Northeast Agr Univ, Minist Educ, Key Lab Dairy Sci, Harbin 150030, Heilongjiang, Peoples R China
基金
黑龙江省自然科学基金;
关键词
Superfine grinding; Whey protein isolate; Transglutaminase; Physicochemical properties; Rheological property; HIGH-INTENSITY ULTRASOUND; MICROBIAL TRANSGLUTAMINASE; SURFACE HYDROPHOBICITY; HEAT-TREATMENT; GELATION; CONCENTRATE; LINKING; GLUTEN;
D O I
10.1016/j.foodchem.2019.125757
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Impacts of superfine grinding treatment (0, 2, 4, 6, 8 or 10 h) on structure, physicochemical and rheological properties of transglutaminase (TGase)-crosslinked whey protein isolate (WPI) were investigated. Size exclusion chromatography showed that high molecular weight polymers were formed in TGase-treated sWPI (WPI treated with superfine grinding), whereas its consumption of free amino groups reached the maximum at grinding 8 h and 10 h. With the milling time extended from 0 to 10 h, particle size of the TGase-crosslinked sWPI gradually increased. Emission spectrum shifted from 338.6 nm to 340.6 nm after sWPI treated with TGase. Meanwhile, TGase-crosslinked sWPI had higher apparent viscosity, emulsifying properties than TGase-crosslinked WPI, but the solubility of TGase-crosslinked sWPI was lower than sWPI. Superfine grinding treatment remarkably increased beta-sheet and random compositions in TGase-crosslinked sWPI. These findings indicated that superfine grinding treatment could enhance the TGase cross-linking degree, and improve rheological properties in TGase-crosslinked WPI.
引用
收藏
页数:8
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