Molecular chaperone-like properties of sodium caseinate to suppress the pressure-induced aggregation of β-lactoglobulin-Reference-Cited by-同舟云学术

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Molecular chaperone-like properties of sodium caseinate to suppress the pressure-induced aggregation of β-lactoglobulin

Published:2019-02-11 Issue:2 Volume:39 Page:210-217
ISSN:0895-7959
Container-title:High Pressure Research
language:en
Short-container-title:High Pressure Research

Author:

He Jin-Song¹,Gao Qing¹,Mu Tai-Hua²,Azuma Norihiro³

Affiliation:

1. College of Food Science and Technology, Yunnan Agricultural University, Kunming, People’s Republic of China

2. Institute of Agro-Food Science & Technology, Chinese Academy of Agricultural Sciences, Beijing, People’s Republic of China

3. Department of Applied Biochemistry, Utsunomiya University, Utsunomiya, Japan

Funder

Yunnan Applied Basic Research Program

National Science Foundation of China

National Natural Science Foundation of China

Publisher

Informa UK Limited

Subject

Condensed Matter Physics

Link

https://www.tandfonline.com/doi/pdf/10.1080/08957959.2019.1575967

Reference25 articles.

1. The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein

2. β-Lactoglobulin Binds Palmitate within Its Central Cavity

3. High pressure-induced changes in bovine milk proteins: A review

4. Effects of high pressure on constituents and properties of milk

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