Scientia Agricultura Sinica ›› 2017, Vol. 50 ›› Issue (13): 2564-2575.doi: 10.3864/j.issn.0578-1752.2017.13.015

• FOOD SCIENCE AND ENGINEERING • Previous Articles     Next Articles

Compositions and Physicochemical Properties of Sweet Almond Isolate Proteins

ZHANG QingAn, ZHANG XinYun, FENG YuLin, SHI FangFang   

  1. School of Food Engineering and Nutrition Sciences, Shaanxi Normal University, Xi'an 710119
  • Received:2016-12-05 Online:2017-07-01 Published:2017-07-01

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Abstract: 【Objective】The aim of this study is to investigate the physical and chemical properties of sweet almond albumin, globulin, gliadin and glutelin. The relationship between the change of protein’s properties and product processing features was also studied to promote the development of high-quality sweet almond products. 【Method】Alkali-solution and Acid-isolation was employed upon the skimmed sweet almond to extract crude protein, and, subsequently, Osborne classification method was adopted to extract the albumin, globulin, gliadin and glutelin. The amino acid composition was determined by Automatic Amino Acid Analyzer. ESEM was used to observe the morphological characteristics of above mentioned proteins; CD spectra scanning was utilized to measure its secondary structure; thermal properties were determined by using DSC and TGA; Rheometer was applied to determine the influence of shear rate, moreover, the linear equation between temperature and viscosity of proteins was determined, and, therefore, the value of Ea and K0 could be calculated.【Result】Various amino acids were detected in isolated proteins derived from sweet almond, containing 17 kinds of amino acids which the human need. It should be noticed that eight kinds of essential amino acids (including histidine) are completely embraced, among which the content of glutamic acid is the highest. Albumin, globulin and gliadin show a state of close aggregation structure, while glutelin shows a state of loose and porous plate. As for the constitution of the secondary structure, alpha helix and random curl are dominant in the isolated proteins compared with other forms of secondary structures. The denaturation temperatures for albumin, globulin, gliadin and glutelin are 62.84, 72.98, 78.33 and 45.70℃, respectively. Therefore, the thermal stability should coincide with the following order: gliadin ＞ globulin ＞ albumin ＞ glutelin. Combined DSC with ESEM, the aggregation degree should conform to the following order: albumin ＞ gliadin ＞globulin ＞ glutelin protein. The aqueous solution of the four kinds of isolated proteins derived from sweet almond are non-newtonian fluid and, furthermore, the relationship between temperature and viscosity is conform to the Arrhenius index equation, and the linear equation matches the parameters in processing well.【Conclusion】Sweet almond isolated protein can be regarded as a high-quality source for plant protein. Results of this study will make greater contributions to the development of sweet almond protein products. Besides, this study definitely do contribution to the function and property control of the protein products derived from sweet almond both in development and processing of the products, which could enhance the additional value and promote the development of sweet almond industry.

Key words: sweet almond, isolate protein, amino acid, thermal properties, rheological properties

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