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WANG Yun-tao, College of Food and Bioengineering, Zhengzhou University of Light Industry, Zhengzhou, Henan 450000 ,China ；Henan Key Laboratory of Cold Chain Food Quality and Safety Control, Zhengzhou, Henan 450000 ,China ；Henan Collaborative Innovation Center for Food Production and Safety, Zhengzhou, Henan 450000 , China
WANG Ying-juan, College of Food and Bioengineering, Zhengzhou University of Light Industry, Zhengzhou, Henan 450000 ,China ；Henan Key Laboratory of Cold Chain Food Quality and Safety Control, Zhengzhou, Henan 450000 ,China ；Henan Collaborative Innovation Center for Food Production and Safety, Zhengzhou, Henan 450000 , China
WANG Jin-feng, College of Food and Bioengineering, Zhengzhou University of Light Industry, Zhengzhou, Henan 450000 ,China ；Henan Key Laboratory of Cold Chain Food Quality and Safety Control, Zhengzhou, Henan 450000 ,China ；Henan Collaborative Innovation Center for Food Production and Safety, Zhengzhou, Henan 450000 , China
BAI Yan-hong, College of Food and Bioengineering, Zhengzhou University of Light Industry, Zhengzhou, Henan 450000 ,China ；Henan Key Laboratory of Cold Chain Food Quality and Safety Control, Zhengzhou, Henan 450000 ,China ；Henan Collaborative Innovation Center for Food Production and Safety, Zhengzhou, Henan 450000 , China
ZHAO Dian-bo, College of Food and Bioengineering, Zhengzhou University of Light Industry, Zhengzhou, Henan 450000 ,China ；Henan Key Laboratory of Cold Chain Food Quality and Safety Control, Zhengzhou, Henan 450000 ,China ；Henan Collaborative Innovation Center for Food Production and Safety, Zhengzhou, Henan 450000 , China

Abstract

In order to improve the functional properties of chickpea protein isolate (CPI), CPI was treated with high intensity ultrasound (HIU) under 450 W for different time(5, 10, 20 min). The emulsifying property of protein was improved obviously by ultrasonic treatment, the solubility of CPI was significantly increased from 7.5 mg/mL to 9.2 mg/mL, and the foaming capacity of CPI was increased to a maximum value of 163.33%. Moreover, the water holding capacity and breaking force of the heat induced CPI gel significantly increased from 58.40% to 75.75%, and 75.7 g to 254.3 g. HIU increased the α-helix content and decreased the β-sheet content of CPI. Moreover, HIU decreased the endogenous fluorescence intensity of the protein and the emission wavelength was red shifted by 5 nm, suggesting that HIU changed the secondary and tertiary structure of CPI. In addition, after ultrasonic treatment, the free sulfhydryl content, surface hydrophobicity and surface potential of CPI were increased. The particle size of CPI gradually decreased with extension of ultrasonic time. These results demonstrate the relationship between the structure and functional properties of CPI.

Publication Date

2-18-2023

First Page

9

Last Page

14, 71

DOI

10.13652/j.issn.1003-5788.2020.08.002

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