Simplified Methods for Purification of Peanut Allergenic Proteins: Ara h 1, Ara h 2, and Ara h 3

Masuyama, Keigo; Yamamoto, Kazutaka; Ito, Kei; Kitagawa, Eiichi; Yamaki, Kohji

doi:10.3136/fstr.20.875

Cited by 12 publications

(2 citation statements)

References 18 publications

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“…A total of 11 types of peanut allergen proteins have been approved by the International Federation of Immunization Nomenclature Subcommittee until now (9), and Ara h1 is the most abundant peanut allergen in peanuts with strong sensitization and a relative molecular mass of 63.5K Da (10,11). Xu et al (12) investigated the Ara h1 secondary structure with the help of circular dichroism (CD) and fluorescence spectroscopy.…”

Section: Introductionmentioning

confidence: 99%

Research on the Structure of Peanut Allergen Protein Ara h1 Based on Aquaphotomics

et al. 2021

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Peanut allergy is becoming a life-threatening disease that could induce severe allergic reactions in modern society, especially for children. The most promising method applied for deallergization is heating pretreatment. However, the mechanism from the view of spectroscopy has not been illustrated. In this study, near-infrared spectroscopy (NIRS) combined with aquaphotomics was introduced to help us understand the detailed structural changes information during the heating process. First, near-infrared (NIR) spectra of Ara h1 were acquired from 25 to 80°C. Then, aquaphotomics processing tools including principal component analysis (PCA), continuous wavelet transform (CWT), and two-dimensional correlation spectroscopy (2D-COS) were utilized for better understanding the thermodynamic changes, secondary structure, and the hydrogen bond network of Ara h1. The results indicated that about 55°C could be a key temperature, which was the structural change point. During the heating process, the hydrogen bond network was destroyed, free water was increased, and the content of protein secondary structure was changed. Moreover, it could reveal the interaction between the water structure and Ara h1 from the perspective of water molecules, and explain the effect of temperature on the Ara h1 structure and hydrogen-bonding system. Thus, this study described a new way to explore the thermodynamic properties of Ara h1 from the perspective of spectroscopy and laid a theoretical foundation for the application of temperature-desensitized protein products.

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Section: Introductionmentioning

confidence: 99%

Research on the Structure of Peanut Allergen Protein Ara h1 Based on Aquaphotomics

et al. 2021

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“…On the one hand, even if chromatography offers extremely high resolution and even the separation of individual peptides, its application in industrial frameworks is not an economically competitive option because of the high costs . Other disadvantages of chromatographic techniques have been identified, such as high time requirements, laborious preparative procedures, possible structural modifications of the peptides, and the difficulties of continuous application at high capacity. − On the other hand, pH precipitation fails to achieve the necessary fractionation efficiencies, and the obtained products have to be reprocessed (by chromatography for example) to attain the desired characteristics because of low yields and variable purities and concentrations. − …”

Section: Introductionmentioning

confidence: 99%

In Silico Evaluation of Ultrafiltration and Nanofiltration Membrane Cascades for Continuous Fractionation of Protein Hydrolysate from Tuna Processing Byproduct

Abejón

Garea

et al. 2016

Ind. Eng. Chem. Res.

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The present work proposes the design of cascades that integrate ultrafiltration (UF) and nanofiltration (NF) membranes to separate the different protein fractions from the protein hydrolysate obtained after hydrolysis of tuna byproducts. Experimental data (permeate flux and rejection of protein fractions under different applied pressures) previously obtained and published by this research group were fitted to empirical models, which were the basis for a process simulation model. High recovery rates (0.9) in the UF stages implied high process yields by reduced desired fraction losses, while similar recovery rates in the NF stages were required for high product purity. However, the applied pressures were not so influential over the performance of the system. Optimization problems were solved to identify the optimal design and operation conditions to maximize the product purity or the process yield. Maximal purity of the preferred 1−4 kDa fraction (49.3% from 19.0% in feed stream) obtained by the configuration with 3 UF stages and another 3 NF stages implied 2 and 5 bar pressures applied in the UF and NF stages, respectively, while 0.9 was the optimal recovery rate value for all the stages. These maximal purity conditions resulted in 62.6% process yield, defined as the percentage of the 1−4 kDa fraction in the feed stream recovered in the product stream. In addition, multiobjective optimization of the process was also carried out to obtain the Pareto graphs that represent the counterbalance between maximal yields and purities.

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Purification and molecular characterization of a truncated-type Ara h 1, a major peanut allergen: oligomer structure, antigenicity, and glycoform

et al. 2021

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Simplified Methods for Purification of Peanut Allergenic Proteins: Ara h 1, Ara h 2, and Ara h 3

Abstract: Simplified methods to purify major peanut allergens (Ara h 1, Ara h 2, and

Cited by 12 publications

References 18 publications

Research on the Structure of Peanut Allergen Protein Ara h1 Based on Aquaphotomics

Research on the Structure of Peanut Allergen Protein Ara h1 Based on Aquaphotomics

In Silico Evaluation of Ultrafiltration and Nanofiltration Membrane Cascades for Continuous Fractionation of Protein Hydrolysate from Tuna Processing Byproduct

Purification and molecular characterization of a truncated-type Ara h 1, a major peanut allergen: oligomer structure, antigenicity, and glycoform

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