Loading…
Temperature dependence of the casein micelle structure in the range of 10–40 °C: An in-situ SAXS study
•The temperature-dependence of the casein micelle was investigated by in-situ SAXS.•SAXS profiles were analyzed using a structure model including water domains.•Inner structure of casein micelles varied sensitively with temperature changes.•The structure changes were thermoreversible. Milk is used a...
Saved in:
Published in: | Food chemistry 2022-11, Vol.393, p.133389-133389, Article 133389 |
---|---|
Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | cdi_FETCH-LOGICAL-c283t-2c8ec319103f85aa98d26db856a0776b81f8d81e080f0539aa82e6fede2500653 |
---|---|
cites | cdi_FETCH-LOGICAL-c283t-2c8ec319103f85aa98d26db856a0776b81f8d81e080f0539aa82e6fede2500653 |
container_end_page | 133389 |
container_issue | |
container_start_page | 133389 |
container_title | Food chemistry |
container_volume | 393 |
creator | Takagi, Hideaki Nakano, Tomoki Aoki, Takayoshi Tanimoto, Morimasa |
description | •The temperature-dependence of the casein micelle was investigated by in-situ SAXS.•SAXS profiles were analyzed using a structure model including water domains.•Inner structure of casein micelles varied sensitively with temperature changes.•The structure changes were thermoreversible.
Milk is used and processed under various environmental temperature, and its physicochemical properties are also strongly affected by temperature. Therefore, it is important to reveal the structure of milk at variable temperatures. In this study, the temperature dependence of the inner structure of bovine casein micelles in the temperature range of 10–40 °C was investigated by in-situ small-angle X-ray scattering (SAXS) method. The micelle size calculated from the SAXS profiles using a micelle model including water domains was almost independent of temperature. The water domain expanded and the distance between the colloidal calcium phosphates (CCP) decreased with increasing temperature. The number of CCPs in a micelle increased, because CCPs were newly formed by the transfer of calcium and inorganic phosphate from serum into the micelle. These structural changes occurred during the cooling process. Therefore, in the temperature range of 10–40 °C, the structure of the casein micelle varied sensitively with the temperature, and these structural changes were thermoreversible in nature. |
doi_str_mv | 10.1016/j.foodchem.2022.133389 |
format | article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2675600785</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0308814622013516</els_id><sourcerecordid>2675600785</sourcerecordid><originalsourceid>FETCH-LOGICAL-c283t-2c8ec319103f85aa98d26db856a0776b81f8d81e080f0539aa82e6fede2500653</originalsourceid><addsrcrecordid>eNqFkE1u2zAQRomiReO6vUKgZTdyh2REjbKKYaRNAQNZ2AGyI2hylNCwJIeUAniXO-QCPULP4KPkJJXiONuuCAzfNz-PsVMOEw5c_VhPyqZx9p6qiQAhJlxKicUHNuKYyzSHXHxkI5CAKfIzdcK-xLgGAAEcP7MTmSksCqFGbL2kakvBtF2gxNGWake1paQpk_aeEmsi-TqpvKXNhpLYhs6-on1x-A-mvnuFObw8PZ_B_s_-7-w8mdY9kEbfdsliervoc53bfWWfSrOJ9O3tHbObn5fL2VU6v_71ezadp1agbFNhkazkBQdZYmZMgU4ot8JMGchztUJeokNOgFBCJgtjUJAqyZHIAFQmx-z7oe82NA8dxVZXPg77m5qaLmqh8kwB5Dig6oDa0MQYqNTb4CsTdpqDHjzrtT561oNnffDcB0_fZnSritx77Ci2By4OAPWXPnoKOlo_mHU-kG21a_z_ZvwDvkqS_Q</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2675600785</pqid></control><display><type>article</type><title>Temperature dependence of the casein micelle structure in the range of 10–40 °C: An in-situ SAXS study</title><source>ScienceDirect Journals</source><creator>Takagi, Hideaki ; Nakano, Tomoki ; Aoki, Takayoshi ; Tanimoto, Morimasa</creator><creatorcontrib>Takagi, Hideaki ; Nakano, Tomoki ; Aoki, Takayoshi ; Tanimoto, Morimasa</creatorcontrib><description>•The temperature-dependence of the casein micelle was investigated by in-situ SAXS.•SAXS profiles were analyzed using a structure model including water domains.•Inner structure of casein micelles varied sensitively with temperature changes.•The structure changes were thermoreversible.
Milk is used and processed under various environmental temperature, and its physicochemical properties are also strongly affected by temperature. Therefore, it is important to reveal the structure of milk at variable temperatures. In this study, the temperature dependence of the inner structure of bovine casein micelles in the temperature range of 10–40 °C was investigated by in-situ small-angle X-ray scattering (SAXS) method. The micelle size calculated from the SAXS profiles using a micelle model including water domains was almost independent of temperature. The water domain expanded and the distance between the colloidal calcium phosphates (CCP) decreased with increasing temperature. The number of CCPs in a micelle increased, because CCPs were newly formed by the transfer of calcium and inorganic phosphate from serum into the micelle. These structural changes occurred during the cooling process. Therefore, in the temperature range of 10–40 °C, the structure of the casein micelle varied sensitively with the temperature, and these structural changes were thermoreversible in nature.</description><identifier>ISSN: 0308-8146</identifier><identifier>EISSN: 1873-7072</identifier><identifier>DOI: 10.1016/j.foodchem.2022.133389</identifier><identifier>PMID: 35689926</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Bovine milk ; Casein micelle ; Colloidal calcium phosphates ; In-situ measurement ; SAXS</subject><ispartof>Food chemistry, 2022-11, Vol.393, p.133389-133389, Article 133389</ispartof><rights>2022 Elsevier Ltd</rights><rights>Copyright © 2022 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c283t-2c8ec319103f85aa98d26db856a0776b81f8d81e080f0539aa82e6fede2500653</citedby><cites>FETCH-LOGICAL-c283t-2c8ec319103f85aa98d26db856a0776b81f8d81e080f0539aa82e6fede2500653</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35689926$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Takagi, Hideaki</creatorcontrib><creatorcontrib>Nakano, Tomoki</creatorcontrib><creatorcontrib>Aoki, Takayoshi</creatorcontrib><creatorcontrib>Tanimoto, Morimasa</creatorcontrib><title>Temperature dependence of the casein micelle structure in the range of 10–40 °C: An in-situ SAXS study</title><title>Food chemistry</title><addtitle>Food Chem</addtitle><description>•The temperature-dependence of the casein micelle was investigated by in-situ SAXS.•SAXS profiles were analyzed using a structure model including water domains.•Inner structure of casein micelles varied sensitively with temperature changes.•The structure changes were thermoreversible.
Milk is used and processed under various environmental temperature, and its physicochemical properties are also strongly affected by temperature. Therefore, it is important to reveal the structure of milk at variable temperatures. In this study, the temperature dependence of the inner structure of bovine casein micelles in the temperature range of 10–40 °C was investigated by in-situ small-angle X-ray scattering (SAXS) method. The micelle size calculated from the SAXS profiles using a micelle model including water domains was almost independent of temperature. The water domain expanded and the distance between the colloidal calcium phosphates (CCP) decreased with increasing temperature. The number of CCPs in a micelle increased, because CCPs were newly formed by the transfer of calcium and inorganic phosphate from serum into the micelle. These structural changes occurred during the cooling process. Therefore, in the temperature range of 10–40 °C, the structure of the casein micelle varied sensitively with the temperature, and these structural changes were thermoreversible in nature.</description><subject>Bovine milk</subject><subject>Casein micelle</subject><subject>Colloidal calcium phosphates</subject><subject>In-situ measurement</subject><subject>SAXS</subject><issn>0308-8146</issn><issn>1873-7072</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><recordid>eNqFkE1u2zAQRomiReO6vUKgZTdyh2REjbKKYaRNAQNZ2AGyI2hylNCwJIeUAniXO-QCPULP4KPkJJXiONuuCAzfNz-PsVMOEw5c_VhPyqZx9p6qiQAhJlxKicUHNuKYyzSHXHxkI5CAKfIzdcK-xLgGAAEcP7MTmSksCqFGbL2kakvBtF2gxNGWake1paQpk_aeEmsi-TqpvKXNhpLYhs6-on1x-A-mvnuFObw8PZ_B_s_-7-w8mdY9kEbfdsliervoc53bfWWfSrOJ9O3tHbObn5fL2VU6v_71ezadp1agbFNhkazkBQdZYmZMgU4ot8JMGchztUJeokNOgFBCJgtjUJAqyZHIAFQmx-z7oe82NA8dxVZXPg77m5qaLmqh8kwB5Dig6oDa0MQYqNTb4CsTdpqDHjzrtT561oNnffDcB0_fZnSritx77Ci2By4OAPWXPnoKOlo_mHU-kG21a_z_ZvwDvkqS_Q</recordid><startdate>20221101</startdate><enddate>20221101</enddate><creator>Takagi, Hideaki</creator><creator>Nakano, Tomoki</creator><creator>Aoki, Takayoshi</creator><creator>Tanimoto, Morimasa</creator><general>Elsevier Ltd</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20221101</creationdate><title>Temperature dependence of the casein micelle structure in the range of 10–40 °C: An in-situ SAXS study</title><author>Takagi, Hideaki ; Nakano, Tomoki ; Aoki, Takayoshi ; Tanimoto, Morimasa</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c283t-2c8ec319103f85aa98d26db856a0776b81f8d81e080f0539aa82e6fede2500653</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Bovine milk</topic><topic>Casein micelle</topic><topic>Colloidal calcium phosphates</topic><topic>In-situ measurement</topic><topic>SAXS</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Takagi, Hideaki</creatorcontrib><creatorcontrib>Nakano, Tomoki</creatorcontrib><creatorcontrib>Aoki, Takayoshi</creatorcontrib><creatorcontrib>Tanimoto, Morimasa</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Takagi, Hideaki</au><au>Nakano, Tomoki</au><au>Aoki, Takayoshi</au><au>Tanimoto, Morimasa</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Temperature dependence of the casein micelle structure in the range of 10–40 °C: An in-situ SAXS study</atitle><jtitle>Food chemistry</jtitle><addtitle>Food Chem</addtitle><date>2022-11-01</date><risdate>2022</risdate><volume>393</volume><spage>133389</spage><epage>133389</epage><pages>133389-133389</pages><artnum>133389</artnum><issn>0308-8146</issn><eissn>1873-7072</eissn><abstract>•The temperature-dependence of the casein micelle was investigated by in-situ SAXS.•SAXS profiles were analyzed using a structure model including water domains.•Inner structure of casein micelles varied sensitively with temperature changes.•The structure changes were thermoreversible.
Milk is used and processed under various environmental temperature, and its physicochemical properties are also strongly affected by temperature. Therefore, it is important to reveal the structure of milk at variable temperatures. In this study, the temperature dependence of the inner structure of bovine casein micelles in the temperature range of 10–40 °C was investigated by in-situ small-angle X-ray scattering (SAXS) method. The micelle size calculated from the SAXS profiles using a micelle model including water domains was almost independent of temperature. The water domain expanded and the distance between the colloidal calcium phosphates (CCP) decreased with increasing temperature. The number of CCPs in a micelle increased, because CCPs were newly formed by the transfer of calcium and inorganic phosphate from serum into the micelle. These structural changes occurred during the cooling process. Therefore, in the temperature range of 10–40 °C, the structure of the casein micelle varied sensitively with the temperature, and these structural changes were thermoreversible in nature.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>35689926</pmid><doi>10.1016/j.foodchem.2022.133389</doi><tpages>1</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0308-8146 |
ispartof | Food chemistry, 2022-11, Vol.393, p.133389-133389, Article 133389 |
issn | 0308-8146 1873-7072 |
language | eng |
recordid | cdi_proquest_miscellaneous_2675600785 |
source | ScienceDirect Journals |
subjects | Bovine milk Casein micelle Colloidal calcium phosphates In-situ measurement SAXS |
title | Temperature dependence of the casein micelle structure in the range of 10–40 °C: An in-situ SAXS study |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-06T17%3A54%3A21IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Temperature%20dependence%20of%20the%20casein%20micelle%20structure%20in%20the%20range%20of%2010%E2%80%9340%C2%A0%C2%B0C:%20An%20in-situ%20SAXS%20study&rft.jtitle=Food%20chemistry&rft.au=Takagi,%20Hideaki&rft.date=2022-11-01&rft.volume=393&rft.spage=133389&rft.epage=133389&rft.pages=133389-133389&rft.artnum=133389&rft.issn=0308-8146&rft.eissn=1873-7072&rft_id=info:doi/10.1016/j.foodchem.2022.133389&rft_dat=%3Cproquest_cross%3E2675600785%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c283t-2c8ec319103f85aa98d26db856a0776b81f8d81e080f0539aa82e6fede2500653%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=2675600785&rft_id=info:pmid/35689926&rfr_iscdi=true |