Effect of high hydrostatic pressure treatment on the structure and physicochemical properties of millet gliadin

Zhang, Yidan; Zhang, Xuebing; Zhang, Zhiheng; Chen, Zhenjia; Xu, Jing; Wang, Xiaowen

doi:10.1016/j.lwt.2021.112755

Cited by 30 publications

(32 citation statements)

References 36 publications

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“…High hydrostatic pressure had an obvious influence on the particle-size distribution, since the average particle size of the mealworm protein solutions treated at 140 to 600 MPa consistently increased compared to the control and the lower pressure level of 70 MPa ( Figure 3 ). This kind of increase in particle-size distribution after HHP treatment was observed previously for different proteins [ 44 , 45 ], and was mainly explained by protein–protein interactions, particularly intermolecular disulfide bond formation and protein aggregate generation [ 46 , 47 , 48 ]. Consequently, the shift in particle-size distribution toward large particle sizes after pressure treatment indicated the formation of mealworm protein aggregates, confirming the results of the turbidity analysis.…”

Section: Discussionsupporting

confidence: 68%

Effect of High Hydrostatic Pressure Intensity on Structural Modifications in Mealworm (Tenebrio molitor) Proteins

Boukil

Marciniak

Mezdour

et al. 2022

Foods

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Processing edible insects into protein extracts may improve consumer acceptability. However, a better understanding of the effects of food processing on the proteins is needed to facilitate their incorporation into food matrices. In this study, soluble proteins from Tenebrio molitor (10% w/v) were pressurized using high hydrostatic pressure (HHP) at 70–600 MPa for 5 min and compared to a non-pressurized control (0.1 MPa). Protein structural modifications were evaluated using turbidity measurement, particle-size distribution, intrinsic fluorescence, surface hydrophobicity, gel electrophoresis coupled with mass spectrometry, and transmission electron microscopy (TEM). The observed decrease in fluorescence intensity, shift in the maximum emission wavelength, and increase in surface hydrophobicity reflected the unfolding of mealworm proteins. The formation of large protein aggregates consisting mainly of hexamerin 2 and ⍺-amylase were confirmed by protein profiles on gel electrophoresis, dynamic light scattering, and TEM analysis. The typical aggregate shape and network observed by TEM after pressurization indicated the potential involvement of myosin and actin in aggregate formation, and these were detected by mass spectrometry. For the first time, the identification of mealworm proteins involved in protein aggregation phenomena under HHP was documented. This work is the first step in understanding the mealworm protein–protein interactions necessary for the development of innovative insect-based ingredients in food formulations.

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Section: Discussionsupporting

confidence: 68%

Effect of High Hydrostatic Pressure Intensity on Structural Modifications in Mealworm (Tenebrio molitor) Proteins

Boukil

Marciniak

Mezdour

et al. 2022

Foods

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“…The high‐pressure destruction of polar and non‐polar covenant bonds with modification of microbial cell structures such as lipids, proteins, and nucleic acid improves the functional properties of food components (Sruthi & Rao, 2021). Zhang, Zhang, et al (2022) investigated the impact of high‐pressure processing on millet gliadin at 100 to 500 MPa for 10 min, and the finding reported that the functional, structural, and stability of millet gliadin are highly influenced by HPP treatment. Moreover, the thermal stability and millet gliadin size were increased with the increased pressure of HPP due to an increase in the β‐sheet concentration of protein molecule.…”

Section: Influence Of Processing Methods On Millet Proteins/peptidesmentioning

confidence: 99%

Influence of processing techniques on the protein quality of major and minor millet crops: A review

Bangar

Suri

Malakar

et al. 2022

Food Processing Preservation

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Millets have a distinctive protein composition comprising of high concentrations of essential amino acids with numerous health‐promoting characteristics. Through various in vitro and animal research studies, a variety of millet‐based bioactive peptides isolated from millets have given significant evidence of their health‐improving properties. However, the processing technique significantly impacts the biological activity of these millet peptides. The amount, structure, and function of major and minor millet proteins are influenced by different processing techniques. Studies have demonstrated that germination and fermentation increase bioavailability, in vitro protein digestibility, and protein efficiency. Moreover, the innovative processing techniques viz: microwave, ultrasound, and high‐pressure processing had a significant impact on structural and quality attributes of the millet proteins and their fractionation. The non‐thermal processing ensured the modification of structure and stability with the enhancement of functionality of the millet protein. The present review has been designed to summarize the major health benefits of millet proteins and the effect of various processing methods on their quality attributes. The information provided in the review would play an important role in further research and development activities at the commercial scale governing the improvement in millet protein efficiency, modification, bioavailability, and in vitro protein digestibility by different processing techniques. Novelty impact statement This review summarized the recent research on the major health benefits of millet proteins and the influence of different processing methods on bioactive peptides from major and minor millets.

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“…The increased UV absorption intensity of DLp treated at 65 °C was due to the exposure of the buried chromophore in the folded protein 33 . Meanwhile, the UV absorption intensity of DLp after UHP treatment exhibits an obvious reduction, demonstrating the varied microenvironments of tyrosine and tryptophan residues 30 . The secondary derivative of UV spectroscopy can further provide information regarding variation in the tertiary conformation of DLp (Fig.…”

Section: Resultsmentioning

confidence: 98%

“…2(a). The CD spectra of DLp showed two negative bands at 208/222 nm and a positive peak around 216 nm representing α‐helices and β‐sheet, respectively 30 . As the heating temperature increased, the molar ellipticity decreased greatly and HT treatment had a significant effect on the CD spectra of DLp, whereas the CD spectra of DLp with UHP treatment were close to the untreated DLp, inferring that the secondary structures of the DLp were greatly affected after HT treatment but not modified significantly upon high‐pressure treatment.…”

Section: Resultsmentioning

confidence: 99%

Contribution of process‐induced molten‐globule state formation in duck liver protein to the enhanced binding ability of (E,E)‐2,4‐heptadienal

Han

Zheng²,

Wang

et al. 2023

J Sci Food Agric

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BACKGROUND Extracted proteins of alternative animal origin tend to present strong off‐flavor perception due to physicochemical interactions of coextracted off‐flavor compounds with proteins. To investigate the relationship between absorption behaviors of volatile aromas and the processes‐induced variations in protein microstructures and molecular conformations, duck liver protein isolate (DLp) was subjected to heating (65/100 °C, 15 min) and ultra‐high pressure (UHP, 100–500 MPa/10 min, 28 °C) treatments to obtain differential unfolded protein states. RESULTS Heat and UHP treatments induced the unfolding of DLp to varied degrees, as revealed by fluorescence spectroscopy, ultraviolet–visible absorption, circular dichroism spectra and surface hydrophobicity measurements. Two types of heating‐denatured states with varied unfolding degrees were obtained, while UHP at both levels of 100/500 MPa caused partial unfolding of DLp and the presence of a molten‐globule state, which significantly enhanced the binding affinity between DLp and (E,E)‐2,4‐heptadienal. In particular, significantly modified secondary structures of DLp were observed in heating‐denatured samples. Excessive denaturing and unfolding degrees resulted in no significant changes in the absorption behavior of the volatile ligand, as characterized by observations of fluorescence quenching and analysis of headspace concentrations. CONCLUSION Defining process‐induced conformational transition behavior of matrix proteins could be a promising strategy to regulate food flavor attributes and, particularly, to produce DLp coextracted with limited off‐flavor components by modifying their interaction during extraction processes. © 2023 Society of Chemical Industry.

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Effect of high hydrostatic pressure treatment on the structure and physicochemical properties of millet gliadin

Cited by 30 publications

References 36 publications

Effect of High Hydrostatic Pressure Intensity on Structural Modifications in Mealworm (Tenebrio molitor) Proteins

Effect of High Hydrostatic Pressure Intensity on Structural Modifications in Mealworm (Tenebrio molitor) Proteins

Influence of processing techniques on the protein quality of major and minor millet crops: A review

Contribution of process‐induced molten‐globule state formation in duck liver protein to the enhanced binding ability of (E,E)‐2,4‐heptadienal

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