Preparation, structure evaluation, and improvement in foaming characteristics of fibrotic pea protein isolate by cold plasma synergistic organic acid treatment
Developing hypoallergenic pea protein isolate (PPI)-based foam stabilizers with high foam stability is of great significance to the nutrition and stability of foamed food in the future food industry. Here, a novel non-thermal fibrosis protein modification technology based on cold plasma synergistic...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Qu, Zihan [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2023transfer abstract |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Constructing heterogeneous conductive network with core-shell AgFe - Jiang, Tao ELSEVIER, 2022, Amsterdam |
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| Übergeordnetes Werk: |
volume:134 ; year:2023 ; pages:0 |
| Links: |
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| DOI / URN: |
10.1016/j.foodhyd.2022.108057 |
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ELV05896312X |
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| 245 | 1 | 0 | |a Preparation, structure evaluation, and improvement in foaming characteristics of fibrotic pea protein isolate by cold plasma synergistic organic acid treatment |
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| 520 | |a Developing hypoallergenic pea protein isolate (PPI)-based foam stabilizers with high foam stability is of great significance to the nutrition and stability of foamed food in the future food industry. Here, a novel non-thermal fibrosis protein modification technology based on cold plasma synergistic tartaric acid (CPA) treatment was used to induce PPI deamidation and thus improve protein solubility, foamability, and foam stability. The results showed that CPA treatment (100 W, 10 min) caused deamidation of approximately 20.02% PPI. The morphology of the CAP-treated PPI aggregate started undergoing fibrosis, with the fiber strip having a length of 7.00–11.00 μm and a width of 0.60–1.00 μm. With CAP treatment, conductivity (111.60 S/m to 129.87 S/m), light transmittance (47.90%–86.90%), foamability (10.00%–112.22%), and foam stability (25.00%–76.82%) significantly increased. Moreover, the thermal denaturation temperature of PPI decreased from 85.29 °C to 82.00 °C. CPA treatment destroyed protein subunits or disulfide bonds and changed the composition and primary structure of PPI. Fourier transform infrared spectroscopy and ultraviolet analysis showed that the α-helix and β-folding contents of the protein's secondary structure were reduced, leading to the unfolding of the rigid structure of PPI, the exposure of hydrophobic groups, and the enhancement of the protein polarityin solution. This research has certain guiding significance and practical value for expanding PPI in the foam food industry and protein membrane field. | ||
| 520 | |a Developing hypoallergenic pea protein isolate (PPI)-based foam stabilizers with high foam stability is of great significance to the nutrition and stability of foamed food in the future food industry. Here, a novel non-thermal fibrosis protein modification technology based on cold plasma synergistic tartaric acid (CPA) treatment was used to induce PPI deamidation and thus improve protein solubility, foamability, and foam stability. The results showed that CPA treatment (100 W, 10 min) caused deamidation of approximately 20.02% PPI. The morphology of the CAP-treated PPI aggregate started undergoing fibrosis, with the fiber strip having a length of 7.00–11.00 μm and a width of 0.60–1.00 μm. With CAP treatment, conductivity (111.60 S/m to 129.87 S/m), light transmittance (47.90%–86.90%), foamability (10.00%–112.22%), and foam stability (25.00%–76.82%) significantly increased. Moreover, the thermal denaturation temperature of PPI decreased from 85.29 °C to 82.00 °C. CPA treatment destroyed protein subunits or disulfide bonds and changed the composition and primary structure of PPI. Fourier transform infrared spectroscopy and ultraviolet analysis showed that the α-helix and β-folding contents of the protein's secondary structure were reduced, leading to the unfolding of the rigid structure of PPI, the exposure of hydrophobic groups, and the enhancement of the protein polarityin solution. This research has certain guiding significance and practical value for expanding PPI in the foam food industry and protein membrane field. | ||
| 650 | 7 | |a Pea protein isolate |2 Elsevier | |
| 650 | 7 | |a Cold plasma |2 Elsevier | |
| 650 | 7 | |a Tartaric acid |2 Elsevier | |
| 650 | 7 | |a Foaming characteristics |2 Elsevier | |
| 650 | 7 | |a Fibrosis modification |2 Elsevier | |
| 700 | 1 | |a Chen, Guiyun |4 oth | |
| 700 | 1 | |a Wang, Jiake |4 oth | |
| 700 | 1 | |a Xie, Xixian |4 oth | |
| 700 | 1 | |a Chen, Ye |4 oth | |
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10.1016/j.foodhyd.2022.108057 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001904.pica (DE-627)ELV05896312X (ELSEVIER)S0268-005X(22)00577-X DE-627 ger DE-627 rakwb eng 670 530 660 VZ 33.68 bkl 35.18 bkl 52.78 bkl Qu, Zihan verfasserin aut Preparation, structure evaluation, and improvement in foaming characteristics of fibrotic pea protein isolate by cold plasma synergistic organic acid treatment 2023transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Developing hypoallergenic pea protein isolate (PPI)-based foam stabilizers with high foam stability is of great significance to the nutrition and stability of foamed food in the future food industry. Here, a novel non-thermal fibrosis protein modification technology based on cold plasma synergistic tartaric acid (CPA) treatment was used to induce PPI deamidation and thus improve protein solubility, foamability, and foam stability. The results showed that CPA treatment (100 W, 10 min) caused deamidation of approximately 20.02% PPI. The morphology of the CAP-treated PPI aggregate started undergoing fibrosis, with the fiber strip having a length of 7.00–11.00 μm and a width of 0.60–1.00 μm. With CAP treatment, conductivity (111.60 S/m to 129.87 S/m), light transmittance (47.90%–86.90%), foamability (10.00%–112.22%), and foam stability (25.00%–76.82%) significantly increased. Moreover, the thermal denaturation temperature of PPI decreased from 85.29 °C to 82.00 °C. CPA treatment destroyed protein subunits or disulfide bonds and changed the composition and primary structure of PPI. Fourier transform infrared spectroscopy and ultraviolet analysis showed that the α-helix and β-folding contents of the protein's secondary structure were reduced, leading to the unfolding of the rigid structure of PPI, the exposure of hydrophobic groups, and the enhancement of the protein polarityin solution. This research has certain guiding significance and practical value for expanding PPI in the foam food industry and protein membrane field. Developing hypoallergenic pea protein isolate (PPI)-based foam stabilizers with high foam stability is of great significance to the nutrition and stability of foamed food in the future food industry. Here, a novel non-thermal fibrosis protein modification technology based on cold plasma synergistic tartaric acid (CPA) treatment was used to induce PPI deamidation and thus improve protein solubility, foamability, and foam stability. The results showed that CPA treatment (100 W, 10 min) caused deamidation of approximately 20.02% PPI. The morphology of the CAP-treated PPI aggregate started undergoing fibrosis, with the fiber strip having a length of 7.00–11.00 μm and a width of 0.60–1.00 μm. With CAP treatment, conductivity (111.60 S/m to 129.87 S/m), light transmittance (47.90%–86.90%), foamability (10.00%–112.22%), and foam stability (25.00%–76.82%) significantly increased. Moreover, the thermal denaturation temperature of PPI decreased from 85.29 °C to 82.00 °C. CPA treatment destroyed protein subunits or disulfide bonds and changed the composition and primary structure of PPI. Fourier transform infrared spectroscopy and ultraviolet analysis showed that the α-helix and β-folding contents of the protein's secondary structure were reduced, leading to the unfolding of the rigid structure of PPI, the exposure of hydrophobic groups, and the enhancement of the protein polarityin solution. This research has certain guiding significance and practical value for expanding PPI in the foam food industry and protein membrane field. Pea protein isolate Elsevier Cold plasma Elsevier Tartaric acid Elsevier Foaming characteristics Elsevier Fibrosis modification Elsevier Chen, Guiyun oth Wang, Jiake oth Xie, Xixian oth Chen, Ye oth Enthalten in Elsevier Jiang, Tao ELSEVIER Constructing heterogeneous conductive network with core-shell AgFe 2022 Amsterdam (DE-627)ELV008810036 volume:134 year:2023 pages:0 https://doi.org/10.1016/j.foodhyd.2022.108057 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 33.68 Oberflächen Dünne Schichten Grenzflächen Physik VZ 35.18 Kolloidchemie Grenzflächenchemie VZ 52.78 Oberflächentechnik Wärmebehandlung VZ AR 134 2023 0 |
| spelling |
10.1016/j.foodhyd.2022.108057 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001904.pica (DE-627)ELV05896312X (ELSEVIER)S0268-005X(22)00577-X DE-627 ger DE-627 rakwb eng 670 530 660 VZ 33.68 bkl 35.18 bkl 52.78 bkl Qu, Zihan verfasserin aut Preparation, structure evaluation, and improvement in foaming characteristics of fibrotic pea protein isolate by cold plasma synergistic organic acid treatment 2023transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Developing hypoallergenic pea protein isolate (PPI)-based foam stabilizers with high foam stability is of great significance to the nutrition and stability of foamed food in the future food industry. Here, a novel non-thermal fibrosis protein modification technology based on cold plasma synergistic tartaric acid (CPA) treatment was used to induce PPI deamidation and thus improve protein solubility, foamability, and foam stability. The results showed that CPA treatment (100 W, 10 min) caused deamidation of approximately 20.02% PPI. The morphology of the CAP-treated PPI aggregate started undergoing fibrosis, with the fiber strip having a length of 7.00–11.00 μm and a width of 0.60–1.00 μm. With CAP treatment, conductivity (111.60 S/m to 129.87 S/m), light transmittance (47.90%–86.90%), foamability (10.00%–112.22%), and foam stability (25.00%–76.82%) significantly increased. Moreover, the thermal denaturation temperature of PPI decreased from 85.29 °C to 82.00 °C. CPA treatment destroyed protein subunits or disulfide bonds and changed the composition and primary structure of PPI. Fourier transform infrared spectroscopy and ultraviolet analysis showed that the α-helix and β-folding contents of the protein's secondary structure were reduced, leading to the unfolding of the rigid structure of PPI, the exposure of hydrophobic groups, and the enhancement of the protein polarityin solution. This research has certain guiding significance and practical value for expanding PPI in the foam food industry and protein membrane field. Developing hypoallergenic pea protein isolate (PPI)-based foam stabilizers with high foam stability is of great significance to the nutrition and stability of foamed food in the future food industry. Here, a novel non-thermal fibrosis protein modification technology based on cold plasma synergistic tartaric acid (CPA) treatment was used to induce PPI deamidation and thus improve protein solubility, foamability, and foam stability. The results showed that CPA treatment (100 W, 10 min) caused deamidation of approximately 20.02% PPI. The morphology of the CAP-treated PPI aggregate started undergoing fibrosis, with the fiber strip having a length of 7.00–11.00 μm and a width of 0.60–1.00 μm. With CAP treatment, conductivity (111.60 S/m to 129.87 S/m), light transmittance (47.90%–86.90%), foamability (10.00%–112.22%), and foam stability (25.00%–76.82%) significantly increased. Moreover, the thermal denaturation temperature of PPI decreased from 85.29 °C to 82.00 °C. CPA treatment destroyed protein subunits or disulfide bonds and changed the composition and primary structure of PPI. Fourier transform infrared spectroscopy and ultraviolet analysis showed that the α-helix and β-folding contents of the protein's secondary structure were reduced, leading to the unfolding of the rigid structure of PPI, the exposure of hydrophobic groups, and the enhancement of the protein polarityin solution. This research has certain guiding significance and practical value for expanding PPI in the foam food industry and protein membrane field. Pea protein isolate Elsevier Cold plasma Elsevier Tartaric acid Elsevier Foaming characteristics Elsevier Fibrosis modification Elsevier Chen, Guiyun oth Wang, Jiake oth Xie, Xixian oth Chen, Ye oth Enthalten in Elsevier Jiang, Tao ELSEVIER Constructing heterogeneous conductive network with core-shell AgFe 2022 Amsterdam (DE-627)ELV008810036 volume:134 year:2023 pages:0 https://doi.org/10.1016/j.foodhyd.2022.108057 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 33.68 Oberflächen Dünne Schichten Grenzflächen Physik VZ 35.18 Kolloidchemie Grenzflächenchemie VZ 52.78 Oberflächentechnik Wärmebehandlung VZ AR 134 2023 0 |
| allfields_unstemmed |
10.1016/j.foodhyd.2022.108057 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001904.pica (DE-627)ELV05896312X (ELSEVIER)S0268-005X(22)00577-X DE-627 ger DE-627 rakwb eng 670 530 660 VZ 33.68 bkl 35.18 bkl 52.78 bkl Qu, Zihan verfasserin aut Preparation, structure evaluation, and improvement in foaming characteristics of fibrotic pea protein isolate by cold plasma synergistic organic acid treatment 2023transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Developing hypoallergenic pea protein isolate (PPI)-based foam stabilizers with high foam stability is of great significance to the nutrition and stability of foamed food in the future food industry. Here, a novel non-thermal fibrosis protein modification technology based on cold plasma synergistic tartaric acid (CPA) treatment was used to induce PPI deamidation and thus improve protein solubility, foamability, and foam stability. The results showed that CPA treatment (100 W, 10 min) caused deamidation of approximately 20.02% PPI. The morphology of the CAP-treated PPI aggregate started undergoing fibrosis, with the fiber strip having a length of 7.00–11.00 μm and a width of 0.60–1.00 μm. With CAP treatment, conductivity (111.60 S/m to 129.87 S/m), light transmittance (47.90%–86.90%), foamability (10.00%–112.22%), and foam stability (25.00%–76.82%) significantly increased. Moreover, the thermal denaturation temperature of PPI decreased from 85.29 °C to 82.00 °C. CPA treatment destroyed protein subunits or disulfide bonds and changed the composition and primary structure of PPI. Fourier transform infrared spectroscopy and ultraviolet analysis showed that the α-helix and β-folding contents of the protein's secondary structure were reduced, leading to the unfolding of the rigid structure of PPI, the exposure of hydrophobic groups, and the enhancement of the protein polarityin solution. This research has certain guiding significance and practical value for expanding PPI in the foam food industry and protein membrane field. Developing hypoallergenic pea protein isolate (PPI)-based foam stabilizers with high foam stability is of great significance to the nutrition and stability of foamed food in the future food industry. Here, a novel non-thermal fibrosis protein modification technology based on cold plasma synergistic tartaric acid (CPA) treatment was used to induce PPI deamidation and thus improve protein solubility, foamability, and foam stability. The results showed that CPA treatment (100 W, 10 min) caused deamidation of approximately 20.02% PPI. The morphology of the CAP-treated PPI aggregate started undergoing fibrosis, with the fiber strip having a length of 7.00–11.00 μm and a width of 0.60–1.00 μm. With CAP treatment, conductivity (111.60 S/m to 129.87 S/m), light transmittance (47.90%–86.90%), foamability (10.00%–112.22%), and foam stability (25.00%–76.82%) significantly increased. Moreover, the thermal denaturation temperature of PPI decreased from 85.29 °C to 82.00 °C. CPA treatment destroyed protein subunits or disulfide bonds and changed the composition and primary structure of PPI. Fourier transform infrared spectroscopy and ultraviolet analysis showed that the α-helix and β-folding contents of the protein's secondary structure were reduced, leading to the unfolding of the rigid structure of PPI, the exposure of hydrophobic groups, and the enhancement of the protein polarityin solution. This research has certain guiding significance and practical value for expanding PPI in the foam food industry and protein membrane field. Pea protein isolate Elsevier Cold plasma Elsevier Tartaric acid Elsevier Foaming characteristics Elsevier Fibrosis modification Elsevier Chen, Guiyun oth Wang, Jiake oth Xie, Xixian oth Chen, Ye oth Enthalten in Elsevier Jiang, Tao ELSEVIER Constructing heterogeneous conductive network with core-shell AgFe 2022 Amsterdam (DE-627)ELV008810036 volume:134 year:2023 pages:0 https://doi.org/10.1016/j.foodhyd.2022.108057 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 33.68 Oberflächen Dünne Schichten Grenzflächen Physik VZ 35.18 Kolloidchemie Grenzflächenchemie VZ 52.78 Oberflächentechnik Wärmebehandlung VZ AR 134 2023 0 |
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10.1016/j.foodhyd.2022.108057 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001904.pica (DE-627)ELV05896312X (ELSEVIER)S0268-005X(22)00577-X DE-627 ger DE-627 rakwb eng 670 530 660 VZ 33.68 bkl 35.18 bkl 52.78 bkl Qu, Zihan verfasserin aut Preparation, structure evaluation, and improvement in foaming characteristics of fibrotic pea protein isolate by cold plasma synergistic organic acid treatment 2023transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Developing hypoallergenic pea protein isolate (PPI)-based foam stabilizers with high foam stability is of great significance to the nutrition and stability of foamed food in the future food industry. Here, a novel non-thermal fibrosis protein modification technology based on cold plasma synergistic tartaric acid (CPA) treatment was used to induce PPI deamidation and thus improve protein solubility, foamability, and foam stability. The results showed that CPA treatment (100 W, 10 min) caused deamidation of approximately 20.02% PPI. The morphology of the CAP-treated PPI aggregate started undergoing fibrosis, with the fiber strip having a length of 7.00–11.00 μm and a width of 0.60–1.00 μm. With CAP treatment, conductivity (111.60 S/m to 129.87 S/m), light transmittance (47.90%–86.90%), foamability (10.00%–112.22%), and foam stability (25.00%–76.82%) significantly increased. Moreover, the thermal denaturation temperature of PPI decreased from 85.29 °C to 82.00 °C. CPA treatment destroyed protein subunits or disulfide bonds and changed the composition and primary structure of PPI. Fourier transform infrared spectroscopy and ultraviolet analysis showed that the α-helix and β-folding contents of the protein's secondary structure were reduced, leading to the unfolding of the rigid structure of PPI, the exposure of hydrophobic groups, and the enhancement of the protein polarityin solution. This research has certain guiding significance and practical value for expanding PPI in the foam food industry and protein membrane field. Developing hypoallergenic pea protein isolate (PPI)-based foam stabilizers with high foam stability is of great significance to the nutrition and stability of foamed food in the future food industry. Here, a novel non-thermal fibrosis protein modification technology based on cold plasma synergistic tartaric acid (CPA) treatment was used to induce PPI deamidation and thus improve protein solubility, foamability, and foam stability. The results showed that CPA treatment (100 W, 10 min) caused deamidation of approximately 20.02% PPI. The morphology of the CAP-treated PPI aggregate started undergoing fibrosis, with the fiber strip having a length of 7.00–11.00 μm and a width of 0.60–1.00 μm. With CAP treatment, conductivity (111.60 S/m to 129.87 S/m), light transmittance (47.90%–86.90%), foamability (10.00%–112.22%), and foam stability (25.00%–76.82%) significantly increased. Moreover, the thermal denaturation temperature of PPI decreased from 85.29 °C to 82.00 °C. CPA treatment destroyed protein subunits or disulfide bonds and changed the composition and primary structure of PPI. Fourier transform infrared spectroscopy and ultraviolet analysis showed that the α-helix and β-folding contents of the protein's secondary structure were reduced, leading to the unfolding of the rigid structure of PPI, the exposure of hydrophobic groups, and the enhancement of the protein polarityin solution. This research has certain guiding significance and practical value for expanding PPI in the foam food industry and protein membrane field. Pea protein isolate Elsevier Cold plasma Elsevier Tartaric acid Elsevier Foaming characteristics Elsevier Fibrosis modification Elsevier Chen, Guiyun oth Wang, Jiake oth Xie, Xixian oth Chen, Ye oth Enthalten in Elsevier Jiang, Tao ELSEVIER Constructing heterogeneous conductive network with core-shell AgFe 2022 Amsterdam (DE-627)ELV008810036 volume:134 year:2023 pages:0 https://doi.org/10.1016/j.foodhyd.2022.108057 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 33.68 Oberflächen Dünne Schichten Grenzflächen Physik VZ 35.18 Kolloidchemie Grenzflächenchemie VZ 52.78 Oberflächentechnik Wärmebehandlung VZ AR 134 2023 0 |
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10.1016/j.foodhyd.2022.108057 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001904.pica (DE-627)ELV05896312X (ELSEVIER)S0268-005X(22)00577-X DE-627 ger DE-627 rakwb eng 670 530 660 VZ 33.68 bkl 35.18 bkl 52.78 bkl Qu, Zihan verfasserin aut Preparation, structure evaluation, and improvement in foaming characteristics of fibrotic pea protein isolate by cold plasma synergistic organic acid treatment 2023transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Developing hypoallergenic pea protein isolate (PPI)-based foam stabilizers with high foam stability is of great significance to the nutrition and stability of foamed food in the future food industry. Here, a novel non-thermal fibrosis protein modification technology based on cold plasma synergistic tartaric acid (CPA) treatment was used to induce PPI deamidation and thus improve protein solubility, foamability, and foam stability. The results showed that CPA treatment (100 W, 10 min) caused deamidation of approximately 20.02% PPI. The morphology of the CAP-treated PPI aggregate started undergoing fibrosis, with the fiber strip having a length of 7.00–11.00 μm and a width of 0.60–1.00 μm. With CAP treatment, conductivity (111.60 S/m to 129.87 S/m), light transmittance (47.90%–86.90%), foamability (10.00%–112.22%), and foam stability (25.00%–76.82%) significantly increased. Moreover, the thermal denaturation temperature of PPI decreased from 85.29 °C to 82.00 °C. CPA treatment destroyed protein subunits or disulfide bonds and changed the composition and primary structure of PPI. Fourier transform infrared spectroscopy and ultraviolet analysis showed that the α-helix and β-folding contents of the protein's secondary structure were reduced, leading to the unfolding of the rigid structure of PPI, the exposure of hydrophobic groups, and the enhancement of the protein polarityin solution. This research has certain guiding significance and practical value for expanding PPI in the foam food industry and protein membrane field. Developing hypoallergenic pea protein isolate (PPI)-based foam stabilizers with high foam stability is of great significance to the nutrition and stability of foamed food in the future food industry. Here, a novel non-thermal fibrosis protein modification technology based on cold plasma synergistic tartaric acid (CPA) treatment was used to induce PPI deamidation and thus improve protein solubility, foamability, and foam stability. The results showed that CPA treatment (100 W, 10 min) caused deamidation of approximately 20.02% PPI. The morphology of the CAP-treated PPI aggregate started undergoing fibrosis, with the fiber strip having a length of 7.00–11.00 μm and a width of 0.60–1.00 μm. With CAP treatment, conductivity (111.60 S/m to 129.87 S/m), light transmittance (47.90%–86.90%), foamability (10.00%–112.22%), and foam stability (25.00%–76.82%) significantly increased. Moreover, the thermal denaturation temperature of PPI decreased from 85.29 °C to 82.00 °C. CPA treatment destroyed protein subunits or disulfide bonds and changed the composition and primary structure of PPI. Fourier transform infrared spectroscopy and ultraviolet analysis showed that the α-helix and β-folding contents of the protein's secondary structure were reduced, leading to the unfolding of the rigid structure of PPI, the exposure of hydrophobic groups, and the enhancement of the protein polarityin solution. This research has certain guiding significance and practical value for expanding PPI in the foam food industry and protein membrane field. Pea protein isolate Elsevier Cold plasma Elsevier Tartaric acid Elsevier Foaming characteristics Elsevier Fibrosis modification Elsevier Chen, Guiyun oth Wang, Jiake oth Xie, Xixian oth Chen, Ye oth Enthalten in Elsevier Jiang, Tao ELSEVIER Constructing heterogeneous conductive network with core-shell AgFe 2022 Amsterdam (DE-627)ELV008810036 volume:134 year:2023 pages:0 https://doi.org/10.1016/j.foodhyd.2022.108057 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 33.68 Oberflächen Dünne Schichten Grenzflächen Physik VZ 35.18 Kolloidchemie Grenzflächenchemie VZ 52.78 Oberflächentechnik Wärmebehandlung VZ AR 134 2023 0 |
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Preparation, structure evaluation, and improvement in foaming characteristics of fibrotic pea protein isolate by cold plasma synergistic organic acid treatment |
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Developing hypoallergenic pea protein isolate (PPI)-based foam stabilizers with high foam stability is of great significance to the nutrition and stability of foamed food in the future food industry. Here, a novel non-thermal fibrosis protein modification technology based on cold plasma synergistic tartaric acid (CPA) treatment was used to induce PPI deamidation and thus improve protein solubility, foamability, and foam stability. The results showed that CPA treatment (100 W, 10 min) caused deamidation of approximately 20.02% PPI. The morphology of the CAP-treated PPI aggregate started undergoing fibrosis, with the fiber strip having a length of 7.00–11.00 μm and a width of 0.60–1.00 μm. With CAP treatment, conductivity (111.60 S/m to 129.87 S/m), light transmittance (47.90%–86.90%), foamability (10.00%–112.22%), and foam stability (25.00%–76.82%) significantly increased. Moreover, the thermal denaturation temperature of PPI decreased from 85.29 °C to 82.00 °C. CPA treatment destroyed protein subunits or disulfide bonds and changed the composition and primary structure of PPI. Fourier transform infrared spectroscopy and ultraviolet analysis showed that the α-helix and β-folding contents of the protein's secondary structure were reduced, leading to the unfolding of the rigid structure of PPI, the exposure of hydrophobic groups, and the enhancement of the protein polarityin solution. This research has certain guiding significance and practical value for expanding PPI in the foam food industry and protein membrane field. |
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Developing hypoallergenic pea protein isolate (PPI)-based foam stabilizers with high foam stability is of great significance to the nutrition and stability of foamed food in the future food industry. Here, a novel non-thermal fibrosis protein modification technology based on cold plasma synergistic tartaric acid (CPA) treatment was used to induce PPI deamidation and thus improve protein solubility, foamability, and foam stability. The results showed that CPA treatment (100 W, 10 min) caused deamidation of approximately 20.02% PPI. The morphology of the CAP-treated PPI aggregate started undergoing fibrosis, with the fiber strip having a length of 7.00–11.00 μm and a width of 0.60–1.00 μm. With CAP treatment, conductivity (111.60 S/m to 129.87 S/m), light transmittance (47.90%–86.90%), foamability (10.00%–112.22%), and foam stability (25.00%–76.82%) significantly increased. Moreover, the thermal denaturation temperature of PPI decreased from 85.29 °C to 82.00 °C. CPA treatment destroyed protein subunits or disulfide bonds and changed the composition and primary structure of PPI. Fourier transform infrared spectroscopy and ultraviolet analysis showed that the α-helix and β-folding contents of the protein's secondary structure were reduced, leading to the unfolding of the rigid structure of PPI, the exposure of hydrophobic groups, and the enhancement of the protein polarityin solution. This research has certain guiding significance and practical value for expanding PPI in the foam food industry and protein membrane field. |
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Developing hypoallergenic pea protein isolate (PPI)-based foam stabilizers with high foam stability is of great significance to the nutrition and stability of foamed food in the future food industry. Here, a novel non-thermal fibrosis protein modification technology based on cold plasma synergistic tartaric acid (CPA) treatment was used to induce PPI deamidation and thus improve protein solubility, foamability, and foam stability. The results showed that CPA treatment (100 W, 10 min) caused deamidation of approximately 20.02% PPI. The morphology of the CAP-treated PPI aggregate started undergoing fibrosis, with the fiber strip having a length of 7.00–11.00 μm and a width of 0.60–1.00 μm. With CAP treatment, conductivity (111.60 S/m to 129.87 S/m), light transmittance (47.90%–86.90%), foamability (10.00%–112.22%), and foam stability (25.00%–76.82%) significantly increased. Moreover, the thermal denaturation temperature of PPI decreased from 85.29 °C to 82.00 °C. CPA treatment destroyed protein subunits or disulfide bonds and changed the composition and primary structure of PPI. Fourier transform infrared spectroscopy and ultraviolet analysis showed that the α-helix and β-folding contents of the protein's secondary structure were reduced, leading to the unfolding of the rigid structure of PPI, the exposure of hydrophobic groups, and the enhancement of the protein polarityin solution. This research has certain guiding significance and practical value for expanding PPI in the foam food industry and protein membrane field. |
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The results showed that CPA treatment (100 W, 10 min) caused deamidation of approximately 20.02% PPI. The morphology of the CAP-treated PPI aggregate started undergoing fibrosis, with the fiber strip having a length of 7.00–11.00 μm and a width of 0.60–1.00 μm. With CAP treatment, conductivity (111.60 S/m to 129.87 S/m), light transmittance (47.90%–86.90%), foamability (10.00%–112.22%), and foam stability (25.00%–76.82%) significantly increased. Moreover, the thermal denaturation temperature of PPI decreased from 85.29 °C to 82.00 °C. CPA treatment destroyed protein subunits or disulfide bonds and changed the composition and primary structure of PPI. Fourier transform infrared spectroscopy and ultraviolet analysis showed that the α-helix and β-folding contents of the protein's secondary structure were reduced, leading to the unfolding of the rigid structure of PPI, the exposure of hydrophobic groups, and the enhancement of the protein polarityin solution. 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