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Molecular and structural properties of three major protein components from almond kernel
Author(s) -
Li Shugang,
Chu Shang,
Lu Jiankang,
Wang Ping,
Ma Meihu
Publication year - 2018
Publication title -
journal of food processing and preservation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.511
H-Index - 48
eISSN - 1745-4549
pISSN - 0145-8892
DOI - 10.1111/jfpp.13536
Subject(s) - glutenin , globulin , kernel (algebra) , storage protein , chemistry , albumin , biochemistry , amino acid , molecular mass , food science , denaturation (fissile materials) , chromatography , biology , mathematics , enzyme , gene , nuclear chemistry , protein subunit , combinatorics , immunology
Three major protein components, namely, albumin, globulin, and glutenin, were extracted from Xinjiang SC‐1 defatted almond kernel powder using the Osborne classification method, and their molecular and structural properties were analyzed. SDS‐PAGE indicated that the molecular weight distribution of almond kernel proteins was within the range of 21–245 kDa. The percentages of essential amino acids in the defatted almond kernel powder, albumin, globulin, and glutenin were 31.17, 24.56, 32.22, and 39.96, respectively. Among the three major protein components, almond albumin had a relatively tighter and more stable structure, resulting in a higher denaturation temperature and lower surface hydrophobicity. Spectroscopic analysis demonstrated that the almond glutenin had more aromatic amino acids distributed on its surface and was more sensitive to ultraviolet and fluorescence spectrums. This information is essential for the understanding and application of almond kernel proteins. Practical applications The present study separated the defatted almond kernel powder into its major protein components, namely, albumin, globulin, and glutenin, and the structural properties of these three major protein components were analyzed. This study aimed to provide essential information for the research and application of the almond kernel proteins.