Molecular and structural properties of three major protein components from almond kernel

Abstract

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 applicationsThe 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.

A versatile ceramic capillary membrane reactor system for continuous enzyme‐catalyzed hydrolysis

“…It is a storage protein belonging to the group of 14S globulins. Almond albumin fraction constitutes 20% of the almond protein isolate while at only 10%, the glutenin protein fraction contributes the smallest amount to the total protein content of almond protein isolate [ 33 ]. Considering the protein composition of pea‐ and almond protein isolate in the RP‐HPLC spectra (Figure 5 ), the large peaks appearing after 50 min can be assigned to the native proteins.…”

Evaluation of the ultrasonically accelerated debitterizing with citric acid solutions of different p H: On the basis of amino acids changes in apricot kernels during debitterizing

“…It has been widely used as food to establish a comprehensive evaluation model based on principal component analysis to evaluate the physical and chemical indexes, bioactive components comprehensively, and flavor components of food from different origins and different processing to compare the quality differences between different products (Chen et al., 2016; Gong et al., 2014; Kang et al., 2017; Xue et al., 2014). This research used the comprehensive evaluation indicators of F1, F2, and F3 to replace the 17 amino acid indicators measured in the comprehensive analysis and established a comprehensive evaluation model with the variance contribution rate corresponding to each principal component (Kang et al., 2017; Li, Chu et al, 2018), that is, F = 0.613 F1 + 0.199 F2 + 0.133 F3. Among them, F is the comprehensive score, 0.613, 0.199, and 0.133 are the contribution rates of the first, the second, and the third principal component, respectively.…”

Effects of ultrasound irradiation on the properties of apricot kernels during accelerated debitterizing

“…DSC is considered to be an important technique for analyzing the thermal properties of proteins; changes in the denaturation temperature and enthalpy can be resolved according to the peak temperature and peak area of the DSC curve. 22 As shown in Fig. 3(F), the thermal denaturation temperatures (T d ) of the apricot kernel proteins before and aer debitterizing are 63.99 C and 70.39 C, respectively.…”

“…A thermal analysis system (Q1000DSC + LNCS + FACS Q600SDT, TA Instruments Co. Ltd., America) was used to investigate the changes in the thermal properties of the proteins. 15,22 To be specic, the protein sample was maintained at 30 C for 1 min and then studied by differential scanning calorimetry (DSC) in the increasing temperature range from 30 C to 140 C at a rate of 10 C min À1 and a nitrogen ow rate of 20 mL min À1 . The thermal denaturation temperatures (T d ) and enthalpy changes (DH) of the samples were calculated according to the soware, respectively.…”

“…The amino acid compositions were determined using a HITACHI L-8900 automatic amino acid analyzer (Hitachi, Tokyo, Japan) according to the ref. 22 and 23. Three replicates were analyzed for each sample.…”