Effects of different mechanical processes on the structural and powdery properties of insoluble undenatured type II collagen

被引:8
|
作者
Wang, Yuan [1 ]
Yang, Shuqiao [1 ]
Zhang, Liang [1 ]
Yuan, Fang [1 ]
Mao, Like [1 ]
Liu, Jinfang [1 ]
Gao, Yanxiang [1 ,2 ]
机构
[1] China Agr Univ, Coll Food Sci & Nutr Engn, China Natl Light Ind Council, Key Lab Hlth Beverages, Beijing 100083, Peoples R China
[2] Box 112,17 Qinghua East Rd, Beijing 100083, Peoples R China
关键词
Insoluble undenatured type II collagen; Mechanical process; Triple helix structure; Wetting rate; Suspension stability; HIGH-PRESSURE MICROFLUIDIZATION; PEPSIN-SOLUBLE COLLAGEN; SKIN; ACID; BEHAVIOR; GELLAN; SCALES; ZEIN;
D O I
10.1016/j.foodchem.2022.135068
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
This study aimed to investigate the effects of dynamic high-pressure homogenization (DHPH), dynamic high-pressure microfluidization (DHPM), and wet media milling (WMM) processes on the particle size, microstruc-ture, triple helix structure, wettability and suspension stability of insoluble undenatured type II collagen (IUC-II). The structural and powdery properties were regulated by different processes and parameters. By contrast, WMM-treated IUC-II showed smallest particle size (15.70 mu m), highest wetting rate (216.94 mm/h) and best suspension stability. However, individual mechanical processes caused partial disruption of IUC-II triple helix structure. Low-acyl gellan gum (LAGG) could bind to IUC-II through hydrogen bonds and hydrophobic interactions, which protected the triple helix structure and further enhanced powdery properties of IUC-II treated by WMM process, but restrained the soluble transition during digestion. These results demonstrated that WMM process was more suitable for enhancing powdery properties of IUC-II, while the triple helix structure of IUC-II could be effectively protected by LAGG.
引用
收藏
页数:12
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