Atmospheric cold plasma treatment of soybean protein isolate: insights into the structural, physicochemical, and allergenic characteristics
Currently, there has been a surge of interest in revealing the interactions between plasma and food matrices. In this study, we investigated the impacts of atmospheric cold plasma (ACP) treatment on the structural, physicochemical and allergenic characteristics of soybean protein isolate (SPI). SPI...
Saved in:
Published in | Journal of food science Vol. 86; no. 1; pp. 68 - 77 |
---|---|
Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
Wiley Subscription Services, Inc
01.01.2021
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | Currently, there has been a surge of interest in revealing the interactions between plasma and food matrices. In this study, we investigated the impacts of atmospheric cold plasma (ACP) treatment on the structural, physicochemical and allergenic characteristics of soybean protein isolate (SPI). SPI dispersions were subjected to ACP treatments at different frequencies (80 to 100 Hz) and durations (1 to 10 min) to investigate the effects of exposing conditions. Results showed that ACP induced reactive oxygen species‐mediated oxidation of soy proteins, resulting in modifications in the secondary and ternary structures of SPI. As a consequence, functional properties of SPI, such as emulsifying (56 to 168%, compared with control) and foaming properties (60 to 194%) were influenced by varying degrees. In addition, under certain circumstance (120 Hz, 5 min), the IgE‐binding level of SPI was decreased by up to 75%, when compared to the control. Moderate treatment yielded products with improved functionality and reduced allergenicity, while extensive exposure induced a loss of vendibility due to protein aggregation.
Practical Application
In this study, we demonstrated for the first time, that plasma species reacted with soybean proteins, resulting in spatial structural changes which are closely related with protein functionality and allergenicity. ACP interacts with macromolecules in aqueous systems and thus can be an alternative and promising nonthermal approach in modifying soybean proteins, whereas the exact role of different processing parameters needs to be well‐elaborated. |
---|---|
AbstractList | Currently, there has been a surge of interest in revealing the interactions between plasma and food matrices. In this study, we investigated the impacts of atmospheric cold plasma (ACP) treatment on the structural, physicochemical and allergenic characteristics of soybean protein isolate (SPI). SPI dispersions were subjected to ACP treatments at different frequencies (80 to 100 Hz) and durations (1 to 10 min) to investigate the effects of exposing conditions. Results showed that ACP induced reactive oxygen species‐mediated oxidation of soy proteins, resulting in modifications in the secondary and ternary structures of SPI. As a consequence, functional properties of SPI, such as emulsifying (56 to 168%, compared with control) and foaming properties (60 to 194%) were influenced by varying degrees. In addition, under certain circumstance (120 Hz, 5 min), the IgE‐binding level of SPI was decreased by up to 75%, when compared to the control. Moderate treatment yielded products with improved functionality and reduced allergenicity, while extensive exposure induced a loss of vendibility due to protein aggregation.
Practical Application
In this study, we demonstrated for the first time, that plasma species reacted with soybean proteins, resulting in spatial structural changes which are closely related with protein functionality and allergenicity. ACP interacts with macromolecules in aqueous systems and thus can be an alternative and promising nonthermal approach in modifying soybean proteins, whereas the exact role of different processing parameters needs to be well‐elaborated. Currently, there has been a surge of interest in revealing the interactions between plasma and food matrices. In this study, we investigated the impacts of atmospheric cold plasma (ACP) treatment on the structural, physicochemical and allergenic characteristics of soybean protein isolate (SPI). SPI dispersions were subjected to ACP treatments at different frequencies (80 to 100 Hz) and durations (1 to 10 min) to investigate the effects of exposing conditions. Results showed that ACP induced reactive oxygen species‐mediated oxidation of soy proteins, resulting in modifications in the secondary and ternary structures of SPI. As a consequence, functional properties of SPI, such as emulsifying (56 to 168%, compared with control) and foaming properties (60 to 194%) were influenced by varying degrees. In addition, under certain circumstance (120 Hz, 5 min), the IgE‐binding level of SPI was decreased by up to 75%, when compared to the control. Moderate treatment yielded products with improved functionality and reduced allergenicity, while extensive exposure induced a loss of vendibility due to protein aggregation. PRACTICAL APPLICATION: In this study, we demonstrated for the first time, that plasma species reacted with soybean proteins, resulting in spatial structural changes which are closely related with protein functionality and allergenicity. ACP interacts with macromolecules in aqueous systems and thus can be an alternative and promising nonthermal approach in modifying soybean proteins, whereas the exact role of different processing parameters needs to be well‐elaborated. Currently, there has been a surge of interest in revealing the interactions between plasma and food matrices. In this study, we investigated the impacts of atmospheric cold plasma (ACP) treatment on the structural, physicochemical and allergenic characteristics of soybean protein isolate (SPI). SPI dispersions were subjected to ACP treatments at different frequencies (80 to 100 Hz) and durations (1 to 10 min) to investigate the effects of exposing conditions. Results showed that ACP induced reactive oxygen species-mediated oxidation of soy proteins, resulting in modifications in the secondary and ternary structures of SPI. As a consequence, functional properties of SPI, such as emulsifying (56 to 168%, compared with control) and foaming properties (60 to 194%) were influenced by varying degrees. In addition, under certain circumstance (120 Hz, 5 min), the IgE-binding level of SPI was decreased by up to 75%, when compared to the control. Moderate treatment yielded products with improved functionality and reduced allergenicity, while extensive exposure induced a loss of vendibility due to protein aggregation. PRACTICAL APPLICATION: In this study, we demonstrated for the first time, that plasma species reacted with soybean proteins, resulting in spatial structural changes which are closely related with protein functionality and allergenicity. ACP interacts with macromolecules in aqueous systems and thus can be an alternative and promising nonthermal approach in modifying soybean proteins, whereas the exact role of different processing parameters needs to be well-elaborated.Currently, there has been a surge of interest in revealing the interactions between plasma and food matrices. In this study, we investigated the impacts of atmospheric cold plasma (ACP) treatment on the structural, physicochemical and allergenic characteristics of soybean protein isolate (SPI). SPI dispersions were subjected to ACP treatments at different frequencies (80 to 100 Hz) and durations (1 to 10 min) to investigate the effects of exposing conditions. Results showed that ACP induced reactive oxygen species-mediated oxidation of soy proteins, resulting in modifications in the secondary and ternary structures of SPI. As a consequence, functional properties of SPI, such as emulsifying (56 to 168%, compared with control) and foaming properties (60 to 194%) were influenced by varying degrees. In addition, under certain circumstance (120 Hz, 5 min), the IgE-binding level of SPI was decreased by up to 75%, when compared to the control. Moderate treatment yielded products with improved functionality and reduced allergenicity, while extensive exposure induced a loss of vendibility due to protein aggregation. PRACTICAL APPLICATION: In this study, we demonstrated for the first time, that plasma species reacted with soybean proteins, resulting in spatial structural changes which are closely related with protein functionality and allergenicity. ACP interacts with macromolecules in aqueous systems and thus can be an alternative and promising nonthermal approach in modifying soybean proteins, whereas the exact role of different processing parameters needs to be well-elaborated. Currently, there has been a surge of interest in revealing the interactions between plasma and food matrices. In this study, we investigated the impacts of atmospheric cold plasma (ACP) treatment on the structural, physicochemical and allergenic characteristics of soybean protein isolate (SPI). SPI dispersions were subjected to ACP treatments at different frequencies (80 to 100 Hz) and durations (1 to 10 min) to investigate the effects of exposing conditions. Results showed that ACP induced reactive oxygen species‐mediated oxidation of soy proteins, resulting in modifications in the secondary and ternary structures of SPI. As a consequence, functional properties of SPI, such as emulsifying (56 to 168%, compared with control) and foaming properties (60 to 194%) were influenced by varying degrees. In addition, under certain circumstance (120 Hz, 5 min), the IgE‐binding level of SPI was decreased by up to 75%, when compared to the control. Moderate treatment yielded products with improved functionality and reduced allergenicity, while extensive exposure induced a loss of vendibility due to protein aggregation.Practical ApplicationIn this study, we demonstrated for the first time, that plasma species reacted with soybean proteins, resulting in spatial structural changes which are closely related with protein functionality and allergenicity. ACP interacts with macromolecules in aqueous systems and thus can be an alternative and promising nonthermal approach in modifying soybean proteins, whereas the exact role of different processing parameters needs to be well‐elaborated. Currently, there has been a surge of interest in revealing the interactions between plasma and food matrices. In this study, we investigated the impacts of atmospheric cold plasma (ACP) treatment on the structural, physicochemical and allergenic characteristics of soybean protein isolate (SPI). SPI dispersions were subjected to ACP treatments at different frequencies (80 to 100 Hz) and durations (1 to 10 min) to investigate the effects of exposing conditions. Results showed that ACP induced reactive oxygen species-mediated oxidation of soy proteins, resulting in modifications in the secondary and ternary structures of SPI. As a consequence, functional properties of SPI, such as emulsifying (56 to 168%, compared with control) and foaming properties (60 to 194%) were influenced by varying degrees. In addition, under certain circumstance (120 Hz, 5 min), the IgE-binding level of SPI was decreased by up to 75%, when compared to the control. Moderate treatment yielded products with improved functionality and reduced allergenicity, while extensive exposure induced a loss of vendibility due to protein aggregation. PRACTICAL APPLICATION: In this study, we demonstrated for the first time, that plasma species reacted with soybean proteins, resulting in spatial structural changes which are closely related with protein functionality and allergenicity. ACP interacts with macromolecules in aqueous systems and thus can be an alternative and promising nonthermal approach in modifying soybean proteins, whereas the exact role of different processing parameters needs to be well-elaborated. |
Author | Zhang, Qiaozhi Cheng, Zhouzhou Wang, Yanbo Nasiru, Mustapha Muhammad Zhang, Jianhao Fu, Linglin |
Author_xml | – sequence: 1 givenname: Qiaozhi surname: Zhang fullname: Zhang, Qiaozhi organization: Zhejiang Gongshang University – sequence: 2 givenname: Zhouzhou surname: Cheng fullname: Cheng, Zhouzhou organization: Zhejiang Gongshang University – sequence: 3 givenname: Jianhao surname: Zhang fullname: Zhang, Jianhao organization: College of Food Science and Technology, Nanjing Agricultural University – sequence: 4 givenname: Mustapha Muhammad surname: Nasiru fullname: Nasiru, Mustapha Muhammad organization: College of Food Science and Technology, Nanjing Agricultural University – sequence: 5 givenname: Yanbo surname: Wang fullname: Wang, Yanbo organization: Zhejiang Gongshang University – sequence: 6 givenname: Linglin orcidid: 0000-0001-5623-3047 surname: Fu fullname: Fu, Linglin email: fulinglin@zjgsu.edu.cn organization: Zhejiang Gongshang University |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/33336377$$D View this record in MEDLINE/PubMed |
BookMark | eNqFkUtv1TAQhS1URG8La3bIEhsWpLXj173sqkJ5qBILYG05zqRx5djBdoTub-BP43BbFpVQZ2PP6DtzNDon6CjEAAi9pOSM1jqnSpCGbTk9o0II-QRt_k2O0IaQtm0o5eoYneR8S9aeyWfomNWSTKkN-n1RppjnEZKz2Ebf49mbPBlcEpgyQSg4DjjHfQcm4DnFAi5gl6M3Bd5hF7K7GUuunxJxGQHnkhZblmT8WzyP--xstCNMzq4DE3psvId0A2H1G00ytlTvXJzNz9HTwfgML-7eU_Tj6sP3y0_N9dePny8vrhvLiZBNr2AYGPTUKjFwJnpKhoG3XFJFFOVC7sD2xHDG1K6HLTXGkLaTnVJU9h2h7BS9Oeyt5_xcIBc9uWzBexMgLlm3ouWt3EkpHkd5dZRK7lhFXz9Ab-OSQj1kpcRWbAnnlXp1Ry3dBL2ek5tM2uv7RCogDoBNMecEg7aumOJiKMk4rynRa_J6zVmvOeu_yVfd-QPd_er_K-RB8ct52D-G6y9X778dhH8A7SG_oQ |
CitedBy_id | crossref_primary_10_1016_j_fochx_2024_101266 crossref_primary_10_1039_D4FB00155A crossref_primary_10_1016_j_fochx_2024_101389 crossref_primary_10_1016_j_foodchem_2022_135316 crossref_primary_10_1016_j_tifs_2024_104529 crossref_primary_10_1016_j_foodchem_2021_130300 crossref_primary_10_1111_jfs_13018 crossref_primary_10_1016_j_fbio_2022_102161 crossref_primary_10_1080_10408398_2023_2295434 crossref_primary_10_1016_j_ifset_2023_103447 crossref_primary_10_1016_j_ijbiomac_2024_133210 crossref_primary_10_1016_j_ifset_2024_103657 crossref_primary_10_1016_j_jafr_2023_100538 crossref_primary_10_1016_j_foodchem_2024_140140 crossref_primary_10_3390_foods12101982 crossref_primary_10_1016_j_ifset_2023_103288 crossref_primary_10_1111_jfpe_14110 crossref_primary_10_1016_j_colsurfb_2022_112516 crossref_primary_10_1016_j_ijbiomac_2023_126098 crossref_primary_10_1007_s11947_022_02842_z crossref_primary_10_1007_s11947_024_03494_x crossref_primary_10_1016_j_foodcont_2024_110537 crossref_primary_10_1016_j_ijbiomac_2023_128556 crossref_primary_10_1016_j_jafr_2024_101383 crossref_primary_10_1007_s11947_023_03159_1 crossref_primary_10_1016_j_foodres_2025_115919 crossref_primary_10_1016_j_focha_2023_100427 crossref_primary_10_3390_pr10122586 crossref_primary_10_1016_j_tifs_2021_10_006 crossref_primary_10_1002_advs_202404131 crossref_primary_10_1007_s11947_024_03368_2 crossref_primary_10_1021_acsfoodscitech_3c00242 crossref_primary_10_1080_02652048_2023_2198030 crossref_primary_10_3390_foods13101522 crossref_primary_10_1007_s12393_023_09348_0 crossref_primary_10_3390_molecules27030601 crossref_primary_10_1016_j_jafr_2023_100821 crossref_primary_10_1111_jfpe_14246 crossref_primary_10_3164_jcbn_22_17 crossref_primary_10_1002_jsfa_13275 crossref_primary_10_1016_j_jafr_2024_101017 crossref_primary_10_1111_jfpe_14680 crossref_primary_10_1016_j_fbio_2023_103434 crossref_primary_10_1016_j_jafr_2024_101177 crossref_primary_10_1016_j_fbio_2024_105014 crossref_primary_10_1080_10408398_2021_2002257 crossref_primary_10_1016_j_fbio_2024_104361 crossref_primary_10_1007_s11694_023_01919_3 crossref_primary_10_1016_j_foodcont_2023_109848 crossref_primary_10_1016_j_ifset_2025_103953 crossref_primary_10_1016_j_lwt_2025_117561 crossref_primary_10_1111_1541_4337_13144 crossref_primary_10_3390_molecules28093882 crossref_primary_10_1016_j_foodres_2024_114575 crossref_primary_10_1016_j_foodres_2023_113565 crossref_primary_10_1016_j_tifs_2022_02_007 crossref_primary_10_1016_j_foodhyd_2024_109973 crossref_primary_10_1016_j_ijbiomac_2024_138407 crossref_primary_10_1016_j_foodchem_2024_140008 crossref_primary_10_1016_j_foodres_2024_115267 crossref_primary_10_1007_s00217_021_03750_w crossref_primary_10_1016_j_foodchem_2021_130809 crossref_primary_10_3390_molecules27010060 crossref_primary_10_1016_j_foodchem_2022_134158 crossref_primary_10_1016_j_ijbiomac_2023_125103 crossref_primary_10_1016_j_ijbiomac_2023_125862 crossref_primary_10_3390_cells11223659 crossref_primary_10_1016_j_fochx_2025_102169 crossref_primary_10_21285_achb_914 crossref_primary_10_1080_10408398_2022_2130161 crossref_primary_10_1007_s11694_023_02347_z crossref_primary_10_3390_molecules28134903 crossref_primary_10_1016_j_foodres_2023_113079 crossref_primary_10_1016_j_afres_2023_100352 crossref_primary_10_1016_j_fufo_2022_100119 crossref_primary_10_1080_10408398_2021_1997907 crossref_primary_10_3389_fnut_2022_809058 crossref_primary_10_1016_j_ifset_2024_103607 crossref_primary_10_3390_foods11091277 crossref_primary_10_3390_foods11182818 |
Cites_doi | 10.1016/j.ifset.2015.03.014 10.1016/j.foodres.2013.02.028 10.1016/j.lwt.2013.05.020 10.1016/j.foodchem.2019.125143 10.1016/j.jaci.2008.09.034 10.1016/j.foodhyd.2016.02.011 10.1093/nar/gkh371 10.1016/j.ifset.2019.02.001 10.1016/j.jfoodeng.2015.05.036 10.1021/acs.jafc.7b02205 10.1016/j.foodchem.2009.02.049 10.1016/j.ifset.2016.08.009 10.1016/j.foodres.2014.10.002 10.1016/j.carbpol.2016.11.050 10.1111/j.1365-2621.1985.tb10572.x 10.1016/j.foodchem.2018.09.068 10.1080/10408398.2015.1045965 10.1016/j.jff.2018.10.019 10.1146/annurev-food-030117-012517 10.1021/jf60217a041 10.1002/ppap.200900077 10.1080/10408398.2017.1335689 10.1016/j.foodchem.2017.03.167 10.1016/0003-9861(59)90090-6 10.1016/S0006-3495(01)76183-8 10.1021/ac9028328 10.1016/j.ifset.2019.102205 10.1016/j.foodchem.2018.11.061 10.1016/j.foodhyd.2014.08.019 10.1016/j.foodres.2015.12.019 10.1016/j.tifs.2016.01.001 10.1016/j.foodchem.2006.08.012 10.1038/srep10031 10.1088/0022-3727/44/47/472001 10.1016/0076-6879(90)86141-H 10.1111/1750-3841.15350 10.1016/j.ifset.2016.06.022 10.1007/s11947-017-2015-z 10.1016/j.ifset.2016.06.007 |
ContentType | Journal Article |
Copyright | 2020 Institute of Food Technologists 2020 Institute of Food Technologists®. 2021 Institute of Food Technologists |
Copyright_xml | – notice: 2020 Institute of Food Technologists – notice: 2020 Institute of Food Technologists®. – notice: 2021 Institute of Food Technologists |
DBID | AAYXX CITATION CGR CUY CVF ECM EIF NPM 7QO 7QR 7ST 7T7 7U7 8FD C1K F28 FR3 K9. NAPCQ P64 RC3 SOI 7X8 7S9 L.6 |
DOI | 10.1111/1750-3841.15556 |
DatabaseName | CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed Biotechnology Research Abstracts Chemoreception Abstracts Environment Abstracts Industrial and Applied Microbiology Abstracts (Microbiology A) Toxicology Abstracts Technology Research Database Environmental Sciences and Pollution Management ANTE: Abstracts in New Technology & Engineering Engineering Research Database ProQuest Health & Medical Complete (Alumni) Nursing & Allied Health Premium Biotechnology and BioEngineering Abstracts Genetics Abstracts Environment Abstracts MEDLINE - Academic AGRICOLA AGRICOLA - Academic |
DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) Technology Research Database Toxicology Abstracts ProQuest Health & Medical Complete (Alumni) Biotechnology and BioEngineering Abstracts Environmental Sciences and Pollution Management Nursing & Allied Health Premium Genetics Abstracts Biotechnology Research Abstracts Chemoreception Abstracts Engineering Research Database Industrial and Applied Microbiology Abstracts (Microbiology A) Environment Abstracts ANTE: Abstracts in New Technology & Engineering MEDLINE - Academic AGRICOLA AGRICOLA - Academic |
DatabaseTitleList | AGRICOLA MEDLINE - Academic Technology Research Database MEDLINE |
Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Economics |
EISSN | 1750-3841 |
EndPage | 77 |
ExternalDocumentID | 33336377 10_1111_1750_3841_15556 JFDS15556 |
Genre | article Journal Article |
GrantInformation_xml | – fundername: National Natural Science Foundation of China funderid: 31871735 – fundername: Zhejiang Provincial Natural Science Foundation for Distinguished Young Scholars of China – fundername: National Natural Science Foundation of China grantid: 31871735 |
GroupedDBID | --- -~X .3N .DC .GA .GJ .Y3 05W 0R~ 10A 1OB 1OC 29K 3-9 31~ 33P 3EH 3SF 4.4 50Y 50Z 51W 51X 52M 52N 52O 52P 52S 52T 52U 52W 52X 53G 5GY 5HH 5LA 5VS 66C 702 7PT 8-0 8-1 8-3 8-4 8-5 8UM 930 A03 AAESR AAEVG AAHBH AAHHS AAHQN AAMNL AANHP AANLZ AAONW AASGY AAXRX AAYCA AAZKR ABCQN ABCUV ABDPE ABEML ABJNI ABPVW ACAHQ ACBNA ACBWZ ACCFJ ACCZN ACFBH ACGFO ACGFS ACGOD ACIWK ACKIV ACPOU ACPRK ACRPL ACSCC ACXBN ACXQS ACYXJ ADBBV ADEOM ADIZJ ADKYN ADMGS ADNMO ADOZA ADXAS ADZMN AEEZP AEGXH AEIGN AEIMD AENEX AEQDE AEUQT AEUYR AFBPY AFFDN AFFPM AFGKR AFPWT AFRAH AFWVQ AFZJQ AHBTC AHEFC AI. AIAGR AITYG AIURR AIWBW AJBDE AJXKR ALAGY ALMA_UNASSIGNED_HOLDINGS ALUQN ALVPJ AMBMR AMYDB ATUGU AUFTA AZBYB AZFZN AZVAB BAFTC BDRZF BFHJK BHBCM BKOMP BMNLL BMXJE BNHUX BROTX BRXPI BY8 CAG COF CS3 D-E D-F D-I DC6 DCZOG DPXWK DR2 DRFUL DROCM DRSTM DU5 EBS EJD ESX F00 F01 F04 F5P FEDTE FZ0 G-S G.N GODZA H.T H.X HF~ HGLYW HVGLF HZ~ IX1 J0M K48 LATKE LC2 LC3 LEEKS LH4 LITHE LOXES LP6 LP7 LUTES LW6 LYRES MEWTI MK4 MRFUL MRSTM MSFUL MSSTM MXFUL MXSTM N04 N05 N9A NEJ NF~ O66 O9- OIG P-O P2P P2W P2X P4D PALCI PQQKQ Q.N Q11 QB0 R.K RIWAO RJQFR RNS ROL RX1 RXW SAMSI SJN SUPJJ TAE TN5 UB1 UBH UHB UKR V8K VH1 W8V W99 WBFHL WBKPD WH7 WIH WIK WOHZO WQJ WRC WXSBR WYISQ XG1 XOL Y6R YQJ ZCA ZCG ZGI ZT4 ZXP ZZTAW ~IA ~KM ~WT AAYXX AEYWJ AGHNM AGQPQ AGYGG CITATION CGR CUY CVF ECM EIF NPM 7QO 7QR 7ST 7T7 7U7 8FD AAMMB AEFGJ AGXDD AIDQK AIDYY C1K F28 FR3 K9. NAPCQ P64 RC3 SOI 7X8 7S9 L.6 |
ID | FETCH-LOGICAL-c4056-d7eff3ed1c75f435d10ff4246170714569ecd0a43379de81aaa02b6b7716db013 |
IEDL.DBID | DR2 |
ISSN | 0022-1147 1750-3841 |
IngestDate | Fri Jul 11 18:37:24 EDT 2025 Fri Jul 11 13:03:14 EDT 2025 Fri Jul 25 10:13:12 EDT 2025 Thu Apr 03 07:03:35 EDT 2025 Thu Apr 24 23:04:52 EDT 2025 Tue Jul 01 02:39:43 EDT 2025 Wed Jan 22 16:32:18 EST 2025 |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 1 |
Keywords | conformational structure soybean protein isolate allergenicity atmosphere cold plasma functional property |
Language | English |
License | 2020 Institute of Food Technologists®. |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c4056-d7eff3ed1c75f435d10ff4246170714569ecd0a43379de81aaa02b6b7716db013 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 |
ORCID | 0000-0001-5623-3047 |
PMID | 33336377 |
PQID | 2475858044 |
PQPubID | 40513 |
PageCount | 10 |
ParticipantIDs | proquest_miscellaneous_2524269665 proquest_miscellaneous_2471467693 proquest_journals_2475858044 pubmed_primary_33336377 crossref_citationtrail_10_1111_1750_3841_15556 crossref_primary_10_1111_1750_3841_15556 wiley_primary_10_1111_1750_3841_15556_JFDS15556 |
ProviderPackageCode | CITATION AAYXX |
PublicationCentury | 2000 |
PublicationDate | January 2021 2021-01-00 2021-Jan 20210101 |
PublicationDateYYYYMMDD | 2021-01-01 |
PublicationDate_xml | – month: 01 year: 2021 text: January 2021 |
PublicationDecade | 2020 |
PublicationPlace | United States |
PublicationPlace_xml | – name: United States – name: Chicago |
PublicationTitle | Journal of food science |
PublicationTitleAlternate | J Food Sci |
PublicationYear | 2021 |
Publisher | Wiley Subscription Services, Inc |
Publisher_xml | – name: Wiley Subscription Services, Inc |
References | 2017; 40 2007; 103 2019; 2019 2015; 5 1959; 82 2020; 85 2011 2019; 52 2015; 167 2017; 65 2019; 58 2019; 300 2017; 232 2016; 38 2016; 37 2016; 58 1990; 186 2014; 66 2009; 116 2010; 82 2001; 80 2004; 32 2018; 9 2015; 29 2015; 81 2013; 54 2017; 11 2015; 44 2017; 57 2013; 52 2016; 157 2009; 123 2011; 44 1978; 26 2018; 51 1985; 50 2016; 49 2010; 7 2019; 274 2018; 58 e_1_2_8_28_1 e_1_2_8_29_1 e_1_2_8_24_1 e_1_2_8_25_1 e_1_2_8_26_1 e_1_2_8_27_1 e_1_2_8_3_1 e_1_2_8_2_1 e_1_2_8_5_1 e_1_2_8_4_1 e_1_2_8_7_1 e_1_2_8_6_1 e_1_2_8_9_1 e_1_2_8_8_1 e_1_2_8_20_1 e_1_2_8_21_1 e_1_2_8_42_1 e_1_2_8_22_1 e_1_2_8_23_1 e_1_2_8_41_1 e_1_2_8_40_1 e_1_2_8_17_1 e_1_2_8_18_1 e_1_2_8_39_1 e_1_2_8_19_1 e_1_2_8_13_1 e_1_2_8_36_1 e_1_2_8_14_1 e_1_2_8_35_1 e_1_2_8_15_1 e_1_2_8_38_1 e_1_2_8_16_1 e_1_2_8_37_1 e_1_2_8_32_1 e_1_2_8_10_1 e_1_2_8_31_1 e_1_2_8_11_1 e_1_2_8_34_1 e_1_2_8_12_1 e_1_2_8_33_1 e_1_2_8_30_1 |
References_xml | – year: 2011 – volume: 57 start-page: 2077 issue: 10 year: 2017 end-page: 2094 article-title: Review of conventional and novel food processing methods on food allergens publication-title: Critical Reviews in Food Science and Nutrition – volume: 103 start-page: 121 issue: 1 year: 2007 end-page: 129 article-title: Peanut protein concentrate: Production and functional properties as affected by processing publication-title: Food Chemistry – volume: 29 start-page: 247 year: 2015 end-page: 254 article-title: Atmospheric pressure cold plasma (ACP) treatment of whey protein isolate model solution publication-title: Innovative Food Science & Emerging Technologies – volume: 52 start-page: 368 year: 2019 end-page: 375 article-title: Effect of cold plasma treatment on the antigenicity of peanut allergen Ara h 1 publication-title: Innovative Food Science & Emerging Technologies – volume: 80 start-page: 2093 issue: 5 year: 2001 end-page: 2109 article-title: Mechanisms of tryptophan fluorescence shifts in proteins publication-title: Biophysical Journal – volume: 50 start-page: 1715 issue: 6 year: 1985 end-page: 1718 article-title: A collaborative study to develop a standardized food protein solubility procedure publication-title: Journal of Food Science – volume: 157 start-page: 1723 year: 2016 end-page: 1731 article-title: Functional and rheological properties of cold plasma treated rice starch publication-title: Carbohydrate Polymers – volume: 116 start-page: 295 issue: 1 year: 2009 end-page: 301 article-title: Oxidative modification of soy protein by peroxyl radicals publication-title: Food Chemistry – volume: 9 start-page: 609 year: 2018 end-page: 629 article-title: Recent advances in the application of cold plasma technology in foods publication-title: Annual Review of Food Science and Technology – volume: 66 start-page: 365 year: 2014 end-page: 372 article-title: Effects of ozone processing on chemical, structural and functional properties of whey protein isolate publication-title: Food Research International – volume: 58 year: 2019 article-title: Effect of cold plasma on the techno‐functional properties of animal protein food ingredients publication-title: Innovative Food Science & Emerging Technologies – volume: 232 start-page: 515 year: 2017 end-page: 522 article-title: Inactivation of soybean trypsin inhibitor by dielectric‐barrier discharge (DBD) plasma publication-title: Food Chemistry – volume: 26 start-page: 716 issue: 3 year: 1978 end-page: 723 article-title: Emulsifying properties of proteins: Evaluation of a turbidimetric technique publication-title: Journal of Agricultural and Food Chemistry – volume: 274 start-page: 789 year: 2019 end-page: 795 article-title: Maillard reaction with ribose, galacto‐oligosaccharide or chitosan‐oligosaccharide reduced the allergenicity of shrimp tropomyosin by inducing conformational changes publication-title: Food Chemistry – volume: 44 start-page: 115 year: 2015 end-page: 121 article-title: Atmospheric pressure cold plasma (ACP) treatment of wheat flour publication-title: Food Hydrocolloids – volume: 123 start-page: 452 issue: 2 year: 2009 end-page: 458.e4 article-title: Soybean ( ) allergy in Europe: Gly m 5 (beta‐conglycinin) and Gly m 6 (glycinin) are potential diagnostic markers for severe allergic reactions to soy publication-title: Journal of Allergy & Clinical Immunology – volume: 82 start-page: 2856 issue: 7 year: 2010 end-page: 2864 article-title: Plasma induced oxidative cleavage of disulfide bonds in polypeptides during nanoelectrospray ionization publication-title: Analytical Chemistry – volume: 37 start-page: 53 year: 2016 end-page: 60 article-title: Influence of low pressure cold plasma on cooking and textural properties of brown rice publication-title: Innovative Food Science & Emerging Technologies – volume: 81 start-page: 50 year: 2015 end-page: 57 article-title: Effect of nonthermal plasma on physico‐chemical, amino acid composition, pasting and protein characteristics of short and long grain rice publication-title: Food Research International – volume: 58 start-page: 49 year: 2016 end-page: 59 article-title: Conjugation of polyphenols prevents lactoferrin from thermal aggregation at neutral pH publication-title: Food Hydrocolloids – volume: 5 year: 2015 article-title: Effects and mechanism of atmospheric‐pressure dielectric barrier discharge cold plasma on lactate dehydrogenase (LDH) enzyme publication-title: Scientific Reports – volume: 52 start-page: 26 issue: 1 year: 2013 end-page: 32 article-title: Effect of oxidation on the emulsifying properties of soy protein isolate publication-title: Food Research International – volume: 85 start-page: 2452 issue: 8 year: 2020 end-page: 2460 article-title: Modification of the physicochemical and structural characteristics of zein suspension by dielectric barrier discharge cold plasma treatment publication-title: Journal of Food Science – volume: 11 start-page: 344 issue: 2 year: 2017 end-page: 354 article-title: Effects of dielectric barrier discharge (DBD) cold plasma treatment on physicochemical and functional properties of peanut protein publication-title: Food & Bioprocess Technology – volume: 2019 start-page: 276 year: 2019 end-page: 283 article-title: Processing chocolate milk drink by low‐pressure cold plasma technology publication-title: Food Chemistry – volume: 38 start-page: 374 year: 2016 end-page: 383 article-title: The effects of pulsed ultraviolet light, cold atmospheric pressure plasma, and gamma‐irradiation on the immunoreactivity of soy protein isolate publication-title: Innovative Food Science & Emerging Technologies – volume: 51 start-page: 121 year: 2018 end-page: 129 article-title: Protein structure modification and allergenic properties of whey proteins upon interaction with tea and coffee phenolic compounds publication-title: Journal of Functional Foods – volume: 82 start-page: 70 issue: 1 year: 1959 end-page: 77 article-title: Tissue sulfhydryl groups publication-title: Archives of Biochemistry and Biophysics – volume: 49 start-page: 24 year: 2016 end-page: 34 article-title: Effect of processing on conformational changes of food proteins related to allergenicity publication-title: Trends in Food Science & Technology – volume: 300 year: 2019 article-title: Altering the IgE binding capacity of king prawn ( ) tropomyosin through conformational changes induced by cold argon‐plasma jet publication-title: Food Chemistry – volume: 65 start-page: 7352 issue: 34 year: 2017 end-page: 7360 article-title: Behaviour of zein in aqueous ethanol under atmospheric pressure cold plasma (ACP) treatment publication-title: Journal of Agricultural & Food Chemistry – volume: 58 start-page: 2583 issue: 15 year: 2018 end-page: 2597 article-title: Cold atmospheric plasma manipulation of proteins in food systems publication-title: Critical Reviews in Food Science and Nutrition – volume: 167 start-page: 166 year: 2015 end-page: 174 article-title: Impact of thermal treatment versus cold atmospheric plasma processing on the techno‐functional protein properties from ‘Salamanca publication-title: Journal of Food Engineering – volume: 54 start-page: 35 issue: 1 year: 2013 end-page: 41 article-title: Determining the effect of UV‐C, high intensity ultrasound and nonthermal atmospheric plasma treatments on reducing the allergenicity of α‐casein and whey proteins publication-title: LWT ‐ Food Science and Technology – volume: 40 start-page: 58 year: 2017 end-page: 67 article-title: High pressure processing assisted enzymatic hydrolysis–An innovative approach for the reduction of soy immunoreactivity publication-title: Innovative Food Science & Emerging Technologies – volume: 186 start-page: 464 issue: 1 year: 1990 end-page: 478 article-title: [49]Determination of carbonyl content in oxidatively modified proteins publication-title: Methods in Enzymology – volume: 44 issue: 47 year: 2011 article-title: Long‐term antibacterial efficacy of air plasma‐activated water publication-title: Journal of Physics D: Applied Physics – volume: 7 start-page: 250 issue: 3‐4 year: 2010 end-page: 257 article-title: The role of acidification for antimicrobial activity of atmospheric pressure plasma in liquids publication-title: Plasma Processes and Polymers – volume: 32 start-page: W668 issue: suppl_2 year: 2004 end-page: W673 article-title: DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data publication-title: Nucleic Acids Research – ident: e_1_2_8_27_1 doi: 10.1016/j.ifset.2015.03.014 – ident: e_1_2_8_3_1 doi: 10.1016/j.foodres.2013.02.028 – ident: e_1_2_8_30_1 doi: 10.1016/j.lwt.2013.05.020 – ident: e_1_2_8_6_1 doi: 10.1016/j.foodchem.2019.125143 – ident: e_1_2_8_9_1 doi: 10.1016/j.jaci.2008.09.034 – ident: e_1_2_8_14_1 doi: 10.1016/j.foodhyd.2016.02.011 – ident: e_1_2_8_38_1 doi: 10.1093/nar/gkh371 – ident: e_1_2_8_36_1 doi: 10.1016/j.ifset.2019.02.001 – ident: e_1_2_8_2_1 doi: 10.1016/j.jfoodeng.2015.05.036 – ident: e_1_2_8_5_1 doi: 10.1021/acs.jafc.7b02205 – ident: e_1_2_8_39_1 doi: 10.1016/j.foodchem.2009.02.049 – ident: e_1_2_8_31_1 doi: 10.1016/j.ifset.2016.08.009 – ident: e_1_2_8_28_1 doi: 10.1016/j.foodres.2014.10.002 – ident: e_1_2_8_32_1 doi: 10.1016/j.carbpol.2016.11.050 – ident: e_1_2_8_18_1 doi: 10.1111/j.1365-2621.1985.tb10572.x – ident: e_1_2_8_8_1 doi: 10.1016/j.foodchem.2018.09.068 – ident: e_1_2_8_35_1 doi: 10.1080/10408398.2015.1045965 – ident: e_1_2_8_24_1 doi: 10.1016/j.jff.2018.10.019 – ident: e_1_2_8_26_1 doi: 10.1146/annurev-food-030117-012517 – ident: e_1_2_8_22_1 doi: 10.1021/jf60217a041 – ident: e_1_2_8_20_1 doi: 10.1002/ppap.200900077 – ident: e_1_2_8_33_1 doi: 10.1080/10408398.2017.1335689 – ident: e_1_2_8_12_1 doi: 10.1016/j.foodchem.2017.03.167 – ident: e_1_2_8_7_1 doi: 10.1016/0003-9861(59)90090-6 – ident: e_1_2_8_37_1 doi: 10.1016/S0006-3495(01)76183-8 – ident: e_1_2_8_40_1 doi: 10.1021/ac9028328 – ident: e_1_2_8_23_1 doi: 10.1016/j.ifset.2019.102205 – ident: e_1_2_8_4_1 doi: 10.1016/j.foodchem.2018.11.061 – ident: e_1_2_8_17_1 doi: 10.1016/j.foodhyd.2014.08.019 – ident: e_1_2_8_21_1 doi: 10.1016/j.foodres.2015.12.019 – ident: e_1_2_8_25_1 doi: 10.1016/j.tifs.2016.01.001 – ident: e_1_2_8_19_1 – ident: e_1_2_8_41_1 doi: 10.1016/j.foodchem.2006.08.012 – ident: e_1_2_8_42_1 doi: 10.1038/srep10031 – ident: e_1_2_8_34_1 doi: 10.1088/0022-3727/44/47/472001 – ident: e_1_2_8_11_1 doi: 10.1016/0076-6879(90)86141-H – ident: e_1_2_8_13_1 doi: 10.1111/1750-3841.15350 – ident: e_1_2_8_15_1 doi: 10.1016/j.ifset.2016.06.022 – ident: e_1_2_8_29_1 – ident: e_1_2_8_10_1 doi: 10.1007/s11947-017-2015-z – ident: e_1_2_8_16_1 doi: 10.1016/j.ifset.2016.06.007 |
SSID | ssj0002236 |
Score | 2.6037812 |
Snippet | Currently, there has been a surge of interest in revealing the interactions between plasma and food matrices. In this study, we investigated the impacts of... |
SourceID | proquest pubmed crossref wiley |
SourceType | Aggregation Database Index Database Enrichment Source Publisher |
StartPage | 68 |
SubjectTerms | Allergenicity Allergens - analysis atmosphere cold plasma Chemical Phenomena Cold plasmas Cold treatment conformational structure Emulsions - chemistry Foaming Food Handling - methods functional property Immunoglobulin E Macromolecules nonthermal processing Oxidation Oxidation-Reduction oxygen Parameter modification Plasma Plasma Gases Process parameters Protein Conformation Protein interaction protein isolates Proteins Reactive oxygen species Reactive Oxygen Species - chemistry soy protein soybean protein isolate Soybean Proteins - chemistry Soybean Proteins - immunology Soybeans Water - chemistry |
Title | Atmospheric cold plasma treatment of soybean protein isolate: insights into the structural, physicochemical, and allergenic characteristics |
URI | https://onlinelibrary.wiley.com/doi/abs/10.1111%2F1750-3841.15556 https://www.ncbi.nlm.nih.gov/pubmed/33336377 https://www.proquest.com/docview/2475858044 https://www.proquest.com/docview/2471467693 https://www.proquest.com/docview/2524269665 |
Volume | 86 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1LT9wwEB5VXOiFFvpKeciVOPRAlmTjx4YbalmhldoDFIlb5FekVSFBynJo_0L_dGecB-xWFCFychJbcZyZzOfxzGeA_dTYTCNwiLmwKubOmjjPRImnglb5hPSBwPTbd3l6wWeXoo8mpFyYlh9icLiRZoT_NSm4Ns09JUe7R8ywPB2hSRREuk0RWwSLzu4IpND4yZ4vHJG_6sh9KJZnpf2yXfoHbC5j12B8pq_A9N1uY05-jm4XZmR_rzA6Puu9XsNGB03ZcStLm_DCV1uw3mcuN2_gz_Hium6Ih2BuGQqQYzeIva81G6LVWV2ypv5lvK5YYICYV2yO0o2A9ojNq4Y8AQ0WFjVD4Mla8loi_jhgrYuF9u8KBAYHTFeO0UYvlB1Kz1tmln4LF9OTH19O424zh9giJpSxU74sM-9Sq0SJGM2lSVlyYrNTlEMlZO6tSzTPMpU7P0m11snYSKNwQufIWfsO1qq68h-A2TyxE4-XLOIP701u8oTb1OcuoWCBMoJR_ykL2zGd04YbV0U_46ExLmiMizDGEXweGty0JB8PV93pZaPotL0pxpxmXZOE8wg-DbdRT2nxRVe-vg11yCjJPPtPHREyi6UUEbxv5W7oT4aHzJSK4DBIz2MdLWbTr-eh9PHJLbbh5ZhCd4KnaQfWUBj8LmKvhdkL6vUXQxgimA |
linkProvider | Wiley-Blackwell |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMw1V1Lb9NAEB6VcigX3g9DgUUCiUMd_Nhdx0gcKkKUPg_QSr2ZfVmKoHYlp0LlL_Bv-Cv8IWbWD0gRIA49kJOTrJPV7szON-OZbwCextqkCoFDyIXJQm6NDvNUlPhW0FM-IZ0nMN3bl7NDvn0kjlbga18L0_JDDAE30gx_XpOCU0D6Jy1Hw0fUsDweoU0Uskus3HFnn9Bta15tTXCPnyXJ9M3B61nYdRYIDQIUGdrMlWXqbGwyUSJgsHFUlpyo1TIq6BEyd8ZGiqdplls3jpVSUaKlztC7sBQ5xN-9BJepjzjx9U_e_qCsQnMre4Zy9DWyjk6IsofOTXjZEv4Cb5fRsjd302vwrV-oNsvlw-h0oUfm8zkOyf9rJa_D1Q59s81WXW7AiqtuwlpfnN3cgi-bi-O6IaqFuWGoI5adoHtxrNiQkM_qkjX1mXaqYp7kYl6xOSowYvaXbF41FOxo8GJRM8TWrOXnJW6TDdZGkahFmedo2GCqsox62VABLP3fMnn2bTi8kLW4A6tVXbl7wEwembHDjwxCLOd0rvOIm9jlNqJ8iDKAUS87henI3KmnyMeid-poTwva08LvaQDPhxtOWh6T3w9d74Wx6A60pkg4OZbjiPMAngxf41FEz5dU5epTP4bsrszTP4wRvnhaShHA3VbQh_mk-JJplgXwwovr3yZabE8n7_zV_X--4zGszQ72dovdrf2dB3AloUwlH1hbh1UUDPcQoeZCP_K6zeD9RavAdxXuf6g |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMw1V1Lb9QwEB6VIkEvvB-BAkYCiUOz5GE7ayQOFcuqD6gQUKm34NiOtCpNVspWqPwFfg1_hV_EjPOALQLEoQf2lN11di17xvPNZOYbgEdxYVKNwCHkwmQht6YIVSpKfCvoKZ-QzhOYvt6TW_t850AcrMDXvham5YcYAm6kGf68JgWf2_InJUe7R8ywPB6hSRSyy6vcdSef0Gtrnm9PcIsfJ8n05fsXW2HXWCA0iE9kaDNXlqmzsclEiXjBxlFZcmJWy6ieR0jljI00T9NMWTeOtdZRUsgiQ-fCUuAQf_ccnOcyUtQtYvL2B2MVWlvZE5Sjq5F1bEKUPHRqwsuG8Bd0uwyWvbWbXoZv_Tq1SS6Ho-NFMTKfT1FI_lcLeQUuddibbbbKchVWXHUNLval2c11-LK5OKobIlqYGYYaYtkcnYsjzYZ0fFaXrKlPCqcr5ikuZhWbofoiYn_GZlVDoY4GLxY1Q2TNWnZeYjbZYG0MiRqUeYaGDaYry6iTDZW_0v8tU2ffgP0zWYubsFrVlbsNzKjIjB1-ZBBgOVeoQkXcxE7ZiLIhygBGvejkpqNyp44iH_PepaM9zWlPc7-nATwZbpi3LCa_H7rey2LeHWdNnnByK8cR5wE8HL7Gg4ieLunK1cd-DFldqdI_jBG-dFpKEcCtVs6H-aT4kmmWBfDUS-vfJprvTCfv_NWdf77jAVx4M5nmr7b3du_CWkJpSj6qtg6rKBfuHuLMRXHfazaDD2etAd8B8rV-Vw |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Atmospheric+cold+plasma+treatment+of+soybean+protein+isolate%3A+insights+into+the+structural%2C+physicochemical%2C+and+allergenic+characteristics&rft.jtitle=Journal+of+food+science&rft.au=Zhang%2C+Qiaozhi&rft.au=Cheng%2C+Zhouzhou&rft.au=Zhang%2C+Jianhao&rft.au=Nasiru%2C+Mustapha+Muhammad&rft.date=2021-01-01&rft.issn=0022-1147&rft.eissn=1750-3841&rft.volume=86&rft.issue=1&rft.spage=68&rft.epage=77&rft_id=info:doi/10.1111%2F1750-3841.15556&rft.externalDBID=10.1111%252F1750-3841.15556&rft.externalDocID=JFDS15556 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0022-1147&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0022-1147&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0022-1147&client=summon |