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Molecules. 2018 Feb 12;23(2). pii: E393. doi: 10.3390/molecules23020393.

Molecular and Functional Properties of Protein Fractions and Isolate from Cashew Nut (Anacardium occidentale L.).

Author information

1
State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, No. 235 Nanjing East Road, Nanchang 330047, China. liuchengmei@aliyun.com.
2
State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, No. 235 Nanjing East Road, Nanchang 330047, China. ncupengqian@163.com.
3
State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, No. 235 Nanjing East Road, Nanchang 330047, China. zhongjunzhen@163.com.
4
State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, No. 235 Nanjing East Road, Nanchang 330047, China. liuwei@ncu.edu.cn.
5
State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, No. 235 Nanjing East Road, Nanchang 330047, China. zhongyejun@ncu.edu.cn.
6
State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, No. 235 Nanjing East Road, Nanchang 330047, China. ncuskwfang@163.com.

Abstract

Some molecular and functional properties of albumin (83.6% protein), globulin (95.5% protein), glutelin (81.3% protein) as well as protein isolate (80.7% protein) from cashew nut were investigated. These proteins were subjected to molecular (circular dichroism, gel electrophoresis, scanning electron microscopy) and functional (solubility, emulsification, foaming, water/oil holding capacity) tests. Cashew nut proteins represent an abundant nutrient with well-balanced amino acid composition and could meet the requirements recommended by FAO/WHO. SDS-PAGE pattern indicated cashew nut proteins were mainly composed of a polypeptide with molecular weight (MW) of 53 kDa, which presented two bands with MW of 32 and 21 kDa under reducing conditions. The far-UV CD spectra indicated that cashew proteins were rich in β-sheets. The surface hydrophobicity of the protein isolate was higher than that of the protein fractions. In pH 7.0, the solubility of protein fractions was above 70%, which was higher than protein isolate at any pH. Glutelin had the highest water/oil holding capacity and foaming properties. Protein isolate displayed better emulsifying properties than protein fractions. In summary, cashew nut kernel proteins have potential as valuable nutrition sources and could be used effectively in the food industry.

KEYWORDS:

cashew nut; functional properties; physicochemical characterization; protein fraction

PMID:
29439533
PMCID:
PMC6016967
DOI:
10.3390/molecules23020393
[Indexed for MEDLINE]
Free PMC Article

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