Characterization and structure of cold-extruded whey protein isolate: impact of ball milling

被引：13

作者：

Yang, Nan ^{[1
,2
]}

Li, Tianqi ^{[1
]}

Ma, Ling ^{[1
]}

Sun, Dongxue ^{[1
]}

Jiang, Zhanmei ^{[1
]}

Hou, Juncai ^{[1
]}

机构：

[1] Northeast Agr Univ, Minist Educ, Key Lab Dairy Sci, Harbin 150030, Heilongjiang, Peoples R China

[2] Heilongjiang Bayi Agr Univ, Coll Food Sci, Daqing 163319, Heilongjiang, Peoples R China

来源：

APPLIED NANOSCIENCE | 2019年 / 9卷 / 03期

基金：

黑龙江省自然科学基金;

关键词：

Whey protein isolate; Cold extrusion; Ball milling; Second structure; Functional properties; DISULFIDE BOND FORMATION; PHYSICOCHEMICAL PROPERTIES; SURFACE HYDROPHOBICITY; EMULSIFYING PROPERTIES; INFRARED-SPECTROSCOPY; MOLECULAR-STRUCTURES; PHYSICAL-PROPERTIES; BETA-LACTOGLOBULIN; CONCENTRATE; HEAT;

D O I：

10.1007/s13204-018-0913-7

中图分类号：

TB3 [工程材料学];

学科分类号：

0805 ; 080502 ;

摘要：

The effect of ball milling on physicochemical, functional and rheological properties and structural characteristics of cold-extruded whey protein isolate (TWPI) was investigated as a function of grinding time. Ball milling decreased the free sulfhydryl content of all the samples. Furthermore, ball milling and cold extrusion could enhance surface hydrophobicity, emulsifying and rheological properties of WPI. The solubility of cold-extruded WPI was far higher than the traditional heat-extruded WPI. The viscoelastic modulus of TWPI, ground by ball milling for 10h, dramatically increased compared to that of WPI at 85 degrees C. Scanning electron microscopy revealed that a ball-milling treatment of 2h remarkably decreased the particle size of all the samples. FTIR demonstrated that ball-milling treatment decreased the ordered secondary structure (-helix and -sheet) of WPI. Therefore, a combination of cold extrusion and ball milling could remarkably enhance the emulsifying and rheological properties of WPI, an effective way for providing novel functional ingredients to the dairy industry.

引用

页码：423 / 433

页数：11

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