High-power sonication of soy proteins: Hydroxyl radicals and their effects on protein structure

dc.contributor.author Rahman, Md Mahfuzur
dc.contributor.author Byanju, Bibek
dc.contributor.author Lamsal, Buddhi
dc.contributor.author Grewell, David
dc.contributor.author Lamsal, Buddhi
dc.contributor.department Food Science and Human Nutrition
dc.date 2020-02-19T17:13:02.000
dc.date.accessioned 2020-06-30T03:59:19Z
dc.date.available 2020-06-30T03:59:19Z
dc.date.copyright Wed Jan 01 00:00:00 UTC 2020
dc.date.embargo 2021-02-10
dc.date.issued 2020-02-10
dc.description.abstract <p>High-power sonication (HPS) is shown to alter protein structure, thus, its functionality, via intermolecular interactions. This study evaluated the effects of HPS on molecular structure of soy proteins in aqueous medium. Free radicals generated during HPS were quantitated using the 5,5-dimethyl-l-pyrrolin N-oxide (DMPO) spin trap method. Electron paramagnetic resonance (EPR) was used to identify them as mostly hydroxyl radicals. The minimum saturation concentration of spin trap solution was determined to be 500 mM of DMPO in water, when exposed to 5 W/cm3 ultrasound power density (PD) for 10 min; subsequently, this concentration was used for quantitating radicals generated in protein samples. Five aqueous soy protein systems, namely, 5% soy protein isolate (SPI), 5% SPI without isoflavonoids (NO-ISO SPI), subunit solutions 1% glycinin (11S) and 1% β conglycinin (7S), and 10% soy flakes (w/v), were sonicated at 2.5 and 5 W/cm3 PDs. Only adducts of hydroxyl radicals (DMPO-OH) were detected in all of these aqueous systems. The highest concentration (3.68 µM) of DMPO-OH adduct was measured in 11S subunit solution at 5 W/cm3, whereas, the lowest (0.67 µM) was in soy flakes solution at 2.5 W/cm3. PD 5 W/cm3 generated higher concentration of radicals in 7S subunit solution, NO-ISO SPI, and soy flakes protein, compared to sonication at PD 2.5 W/cm3. No change in the protein electrophoretic patterns were observed due to HPS. However, some changes due to HPS were observed in the estimated secondary and tertiary structures, and the contents of free sulfhydryl groups and disulfide bonds in proteins.</p>
dc.description.comments <p>This accepted article is published as Rahman, M.d.M., Byanju, B., Grewell, D., Lamsal, B.P. High-power sonication of soy proteins: Hydroxyl radicals and their effects on protein structure. <em>Ultrasonics Sonochemistry</em>, Feb 2020, 64 (June 2020); 105019. DOI: <a target="_blank">10.1016/j.ultsonch.2020.105019</a>. Posted with permission.</p>
dc.format.mimetype application/pdf
dc.identifier archive/lib.dr.iastate.edu/fshn_ag_pubs/223/
dc.identifier.articleid 1223
dc.identifier.contextkey 16594048
dc.identifier.s3bucket isulib-bepress-aws-west
dc.identifier.submissionpath fshn_ag_pubs/223
dc.identifier.uri https://dr.lib.iastate.edu/handle/20.500.12876/37520
dc.language.iso en
dc.source.bitstream archive/lib.dr.iastate.edu/fshn_ag_pubs/223/2020_GS_Alert___LamsalBP_High_power_sonication_of_soy.pdf|||Fri Jan 14 22:42:59 UTC 2022
dc.source.uri 10.1016/j.ultsonch.2020.105019
dc.subject.disciplines Agricultural Science
dc.subject.disciplines Amino Acids, Peptides, and Proteins
dc.subject.disciplines Food Science
dc.subject.disciplines Human and Clinical Nutrition
dc.subject.keywords High power sonication
dc.subject.keywords Soy protein
dc.subject.keywords Spin trapping
dc.subject.keywords Hydroxyl radicals
dc.subject.keywords Protein oxidation
dc.subject.keywords Protein structure
dc.title High-power sonication of soy proteins: Hydroxyl radicals and their effects on protein structure
dc.type article
dc.type.genre article
dspace.entity.type Publication
relation.isAuthorOfPublication 344615fd-7cc2-4855-9a09-7c0f3d631a0c
relation.isOrgUnitOfPublication 4b6428c6-1fda-4a40-b375-456d49d2fb80
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