Studies on the shape of casein particle and its denaturation in milk I

The normal shape and its denaturation of the casein particle in milk was investigated with the 50kV. electron-microscope. Principal results obtained are as follows: 1) The size of casein particles was about 20 to 200 mμ in diameter in cow's and goat's milk, but it was much smaller in human...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Nihon Chikusan Gakkaiho 1956, Vol.27(1), pp.39-42
Hauptverfasser: MAENO, MASAHISA, YUSA, KOGO
Format: Artikel
Sprache:jpn
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 42
container_issue 1
container_start_page 39
container_title Nihon Chikusan Gakkaiho
container_volume 27
creator MAENO, MASAHISA
YUSA, KOGO
description The normal shape and its denaturation of the casein particle in milk was investigated with the 50kV. electron-microscope. Principal results obtained are as follows: 1) The size of casein particles was about 20 to 200 mμ in diameter in cow's and goat's milk, but it was much smaller in human milk than in cow's milk. 2) Some absorbed substance was observed around casein particles in the normal milk and seemed to have some relationship with calcium in milk. 3) At the iso-electric point of casein in milk, same casein particles were agglutinated, forming bigger particles, and the absorbed substance observed around the original casein particles disappeared in the newly formed particles. At pH 2.4, the casein particles underwent transformation and looked like "swelling particles", 4) When the pH value was adjusted to normal by adding alkali, these acid-denaturated, casein particles did not restored their original shape. Accordingly, this type of transformation was irreversible.
doi_str_mv 10.2508/chikusan.27.39
format Article
fullrecord <record><control><sourceid>jstage_cross</sourceid><recordid>TN_cdi_crossref_primary_10_2508_chikusan_27_39</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>article_chikusan1924_27_1_27_1_39_article_char_en</sourcerecordid><originalsourceid>FETCH-LOGICAL-c2009-f6994ce7c3ab9b4f2cca1e7d88258b3c06e6fbcb15ea69f8ce25fef170ca39453</originalsourceid><addsrcrecordid>eNpNkE1LAzEQhoMoWGqvnvMHds3H7iY5SrG1UPCggrcwm53Y2HZbkvTgv3dLP_AyM4fnGWZeQh45K0XN9JNbhfUhQV8KVUpzQ0Zca1ZoUde3wyyrpjBMfd2TSUqhZUxyxZkSIzJ7z4cuYKK7nuYV0rSCPdKdpw4Shp7uIebgNkih72jIiXbYQz5EyGEwBmAbNmu6eCB3HjYJJ-c-Jp-zl4_pa7F8my-mz8vCCcZM4RtjKofKSWhNW3nhHHBUnR4O1a10rMHGt67lNUJjvHYoao-eK-ZAmqqWY1Ke9rq4Symit_sYthB_LWf2GIS9BGGFstIMwvwk_KQM33jFz29dcW5EdVT4qUjzj4BosZd_igNtvw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Studies on the shape of casein particle and its denaturation in milk I</title><source>Alma/SFX Local Collection</source><creator>MAENO, MASAHISA ; YUSA, KOGO</creator><creatorcontrib>MAENO, MASAHISA ; YUSA, KOGO</creatorcontrib><description>The normal shape and its denaturation of the casein particle in milk was investigated with the 50kV. electron-microscope. Principal results obtained are as follows: 1) The size of casein particles was about 20 to 200 mμ in diameter in cow's and goat's milk, but it was much smaller in human milk than in cow's milk. 2) Some absorbed substance was observed around casein particles in the normal milk and seemed to have some relationship with calcium in milk. 3) At the iso-electric point of casein in milk, same casein particles were agglutinated, forming bigger particles, and the absorbed substance observed around the original casein particles disappeared in the newly formed particles. At pH 2.4, the casein particles underwent transformation and looked like "swelling particles", 4) When the pH value was adjusted to normal by adding alkali, these acid-denaturated, casein particles did not restored their original shape. Accordingly, this type of transformation was irreversible.</description><identifier>ISSN: 1346-907X</identifier><identifier>EISSN: 1880-8255</identifier><identifier>DOI: 10.2508/chikusan.27.39</identifier><language>jpn</language><publisher>Japanese Society of Animal Science</publisher><ispartof>Nihon Chikusan Gakkaiho, 1956, Vol.27(1), pp.39-42</ispartof><rights>Japanese Society of Animal Science</rights><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,4024,27923,27924,27925</link.rule.ids></links><search><creatorcontrib>MAENO, MASAHISA</creatorcontrib><creatorcontrib>YUSA, KOGO</creatorcontrib><title>Studies on the shape of casein particle and its denaturation in milk I</title><title>Nihon Chikusan Gakkaiho</title><addtitle>Nihon Chikusan Gakkaiho</addtitle><description>The normal shape and its denaturation of the casein particle in milk was investigated with the 50kV. electron-microscope. Principal results obtained are as follows: 1) The size of casein particles was about 20 to 200 mμ in diameter in cow's and goat's milk, but it was much smaller in human milk than in cow's milk. 2) Some absorbed substance was observed around casein particles in the normal milk and seemed to have some relationship with calcium in milk. 3) At the iso-electric point of casein in milk, same casein particles were agglutinated, forming bigger particles, and the absorbed substance observed around the original casein particles disappeared in the newly formed particles. At pH 2.4, the casein particles underwent transformation and looked like "swelling particles", 4) When the pH value was adjusted to normal by adding alkali, these acid-denaturated, casein particles did not restored their original shape. Accordingly, this type of transformation was irreversible.</description><issn>1346-907X</issn><issn>1880-8255</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1956</creationdate><recordtype>article</recordtype><recordid>eNpNkE1LAzEQhoMoWGqvnvMHds3H7iY5SrG1UPCggrcwm53Y2HZbkvTgv3dLP_AyM4fnGWZeQh45K0XN9JNbhfUhQV8KVUpzQ0Zca1ZoUde3wyyrpjBMfd2TSUqhZUxyxZkSIzJ7z4cuYKK7nuYV0rSCPdKdpw4Shp7uIebgNkih72jIiXbYQz5EyGEwBmAbNmu6eCB3HjYJJ-c-Jp-zl4_pa7F8my-mz8vCCcZM4RtjKofKSWhNW3nhHHBUnR4O1a10rMHGt67lNUJjvHYoao-eK-ZAmqqWY1Ke9rq4Symit_sYthB_LWf2GIS9BGGFstIMwvwk_KQM33jFz29dcW5EdVT4qUjzj4BosZd_igNtvw</recordid><startdate>1956</startdate><enddate>1956</enddate><creator>MAENO, MASAHISA</creator><creator>YUSA, KOGO</creator><general>Japanese Society of Animal Science</general><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>1956</creationdate><title>Studies on the shape of casein particle and its denaturation in milk I</title><author>MAENO, MASAHISA ; YUSA, KOGO</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2009-f6994ce7c3ab9b4f2cca1e7d88258b3c06e6fbcb15ea69f8ce25fef170ca39453</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>jpn</language><creationdate>1956</creationdate><toplevel>online_resources</toplevel><creatorcontrib>MAENO, MASAHISA</creatorcontrib><creatorcontrib>YUSA, KOGO</creatorcontrib><collection>CrossRef</collection><jtitle>Nihon Chikusan Gakkaiho</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>MAENO, MASAHISA</au><au>YUSA, KOGO</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Studies on the shape of casein particle and its denaturation in milk I</atitle><jtitle>Nihon Chikusan Gakkaiho</jtitle><addtitle>Nihon Chikusan Gakkaiho</addtitle><date>1956</date><risdate>1956</risdate><volume>27</volume><issue>1</issue><spage>39</spage><epage>42</epage><pages>39-42</pages><issn>1346-907X</issn><eissn>1880-8255</eissn><abstract>The normal shape and its denaturation of the casein particle in milk was investigated with the 50kV. electron-microscope. Principal results obtained are as follows: 1) The size of casein particles was about 20 to 200 mμ in diameter in cow's and goat's milk, but it was much smaller in human milk than in cow's milk. 2) Some absorbed substance was observed around casein particles in the normal milk and seemed to have some relationship with calcium in milk. 3) At the iso-electric point of casein in milk, same casein particles were agglutinated, forming bigger particles, and the absorbed substance observed around the original casein particles disappeared in the newly formed particles. At pH 2.4, the casein particles underwent transformation and looked like "swelling particles", 4) When the pH value was adjusted to normal by adding alkali, these acid-denaturated, casein particles did not restored their original shape. Accordingly, this type of transformation was irreversible.</abstract><pub>Japanese Society of Animal Science</pub><doi>10.2508/chikusan.27.39</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 1346-907X
ispartof Nihon Chikusan Gakkaiho, 1956, Vol.27(1), pp.39-42
issn 1346-907X
1880-8255
language jpn
recordid cdi_crossref_primary_10_2508_chikusan_27_39
source Alma/SFX Local Collection
title Studies on the shape of casein particle and its denaturation in milk I
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-06T08%3A52%3A48IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstage_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Studies%20on%20the%20shape%20of%20casein%20particle%20and%20its%20denaturation%20in%20milk%20I&rft.jtitle=Nihon%20Chikusan%20Gakkaiho&rft.au=MAENO,%20MASAHISA&rft.date=1956&rft.volume=27&rft.issue=1&rft.spage=39&rft.epage=42&rft.pages=39-42&rft.issn=1346-907X&rft.eissn=1880-8255&rft_id=info:doi/10.2508/chikusan.27.39&rft_dat=%3Cjstage_cross%3Earticle_chikusan1924_27_1_27_1_39_article_char_en%3C/jstage_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true