Structure of Human Serum Albumin at a Foam Surface

Enomoto, Kanta; Torisu, Tetsuo; Mizuguchi, Junya; Tanoue, Ryosuke; Uchiyama, Susumu

doi:https://doi.org/10.1021/acs.jafc.3c09357

Structure of Human Serum Albumin at a Foam Surface

Enomoto, Kanta; Torisu, Tetsuo; Mizuguchi, Junya et al.

Journal of Agricultural and Food Chemistry, 2024, 72(15), 8774-8783

アクセス数:631件（2025-07-27 09:30 集計）

固定URL: https://hdl.handle.net/11094/95448

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タイトル	Structure of Human Serum Albumin at a Foam Surface
著者	著者名 Enomoto, Kanta
	NRID 1000010730492 1000010730492 ORCID 0000-0002-8269-7803 0000-0002-8269-7803 researchmap permalink torisutetsuo torisutetsuo Scopus Author ID 57361287600 57361287600 著者名 Torisu, Tetsuo
	著者名 Mizuguchi, Junya
	著者名 Tanoue, Ryosuke
	NRID 1000090335381 1000090335381 ORCID 0000-0002-5181-179X 0000-0002-5181-179X researchmap permalink read0090387 read0090387 Scopus Author ID 35429790100 35429790100 著者名 Uchiyama, Susumu
キーワード等	air-water interface
	foam
	hydrogen/deuterium exchange mass spectrometry
	protein structure
内容	Enomoto K., Torisu T., Mizuguchi J., et al. Structure of Human Serum Albumin at a Foam Surface. Journal of Agricultural and Food Chemistry 72, 8774 (2024); https://doi.org/10.1021/acs.jafc.3c09357.
抄録	Proteins can be adsorbed on the air-water interface (AWI), and the structural changes in proteins at the AWI are closely related to the foaming properties of foods and beverages. However, how these structural changes in proteins at the AWI occur is not well understood. We developed a method for the structural assessment of proteins in the foam state using hydrogen/deuterium exchange mass spectrometry. Adsorption sites and structural changes in human serum albumin (HSA) were identified in situ at the peptide-level resolution. The N-terminus and the loop (E492-T506), which contains hydrophobic amino acids, were identified as adsorption sites. Both the structural flexibility and hydrophobicity were considered to be critical factors for the adsorption of HSA at the AWI. Structural changes in HSA were observed after more than one minute of foaming and were spread widely throughout the structure. These structural changes at the foam AWI were reversible.
出版者	American Chemical Society
収録物名	Journal of Agricultural and Food Chemistry
巻(号)	72(15)
ページ	8774-8783
刊行年月	2024-04-17
言語	英語
ハンドルURL	https://hdl.handle.net/11094/95448
PISSN	00218561
eISSN	15205118
関連情報 (isVersionOf)	DOI (出版社版) https://doi.org/10.1021/acs.jafc.3c09357
アクセス権	open access
権利情報	This document is the Accepted Manuscript version of a Published Work that appeared in final form in Journal of Agricultural and Food Chemistry, © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://doi.org/10.1021/acs.jafc.3c09357.
出版タイプ	Accepted Manuscript
カテゴリ	学術雑誌論文 Journal Article

資源タイプ	学術雑誌論文
ローカル資源タイプ	学術雑誌論文
DCMI資源タイプ	text
DCTERMS.bibliographicCitation	Journal of Agricultural and Food Chemistry. 2024, 72(15), p. 8774-8783
DC.title	Structure of Human Serum Albumin at a Foam Surface
DC.creator	Enomoto, Kanta
	Torisu, Tetsuo
	Mizuguchi, Junya
	Tanoue, Ryosuke
	Uchiyama, Susumu
DC.publisher	American Chemical Society
DC.language' scheme='DCTERMS.RFC1766	英語
DC.type' scheme='DCTERMS.DCMIType	text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2024-04-17
DC.identifier	https://doi.org/10.1021/acs.jafc.3c09357
DC.subject	air-water interface
	foam
	hydrogen/deuterium exchange mass spectrometry
	protein structure
DC.description	Enomoto K., Torisu T., Mizuguchi J., et al. Structure of Human Serum Albumin at a Foam Surface. Journal of Agricultural and Food Chemistry 72, 8774 (2024); https://doi.org/10.1021/acs.jafc.3c09357.
DCTERMS.abstract	Proteins can be adsorbed on the air-water interface (AWI), and the structural changes in proteins at the AWI are closely related to the foaming properties of foods and beverages. However, how these structural changes in proteins at the AWI occur is not well understood. We developed a method for the structural assessment of proteins in the foam state using hydrogen/deuterium exchange mass spectrometry. Adsorption sites and structural changes in human serum albumin (HSA) were identified in situ at the peptide-level resolution. The N-terminus and the loop (E492-T506), which contains hydrophobic amino acids, were identified as adsorption sites. Both the structural flexibility and hydrophobicity were considered to be critical factors for the adsorption of HSA at the AWI. Structural changes in HSA were observed after more than one minute of foaming and were spread widely throughout the structure. These structural changes at the foam AWI were reversible.
DC.rights	This document is the Accepted Manuscript version of a Published Work that appeared in final form in Journal of Agricultural and Food Chemistry, © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://doi.org/10.1021/acs.jafc.3c09357.
DC.format	95448
citation_title	Structure of Human Serum Albumin at a Foam Surface
citation_author	Enomoto, Kanta
	Torisu, Tetsuo
	Mizuguchi, Junya
	Tanoue, Ryosuke
	Uchiyama, Susumu
citation_publisher	American Chemical Society
citation_language	英語
citation_date	2024-04-17
citation_journal_title	Journal of Agricultural and Food Chemistry
citation_volume	72
citation_issue	15
citation_firstpage	8774
citation_lastpage	8783
citation_doi	https://doi.org/10.1021/acs.jafc.3c09357
citation_public_url	https://hdl.handle.net/11094/95448

Structure of Human Serum Albumin at a Foam Surface

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