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Effects of supercritical carbon dioxide treatment for sterilization purpose on meat quality of porcine longissimus dorsi muscle

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dc.contributor.authorChoi, Y. M.-
dc.contributor.authorRyu, Y. C.-
dc.contributor.authorLee, S. H.-
dc.contributor.authorGo, G. W.-
dc.contributor.authorShin, H. G.-
dc.contributor.authorKim, K. H.-
dc.contributor.authorRhee, M. S.-
dc.contributor.authorKim, B. C.-
dc.date.accessioned2021-09-09T16:33:16Z-
dc.date.available2021-09-09T16:33:16Z-
dc.date.created2021-06-15-
dc.date.issued2008-
dc.identifier.issn0023-6438-
dc.identifier.urihttps://scholar.korea.ac.kr/handle/2021.sw.korea/125555-
dc.description.abstractThe objective of this study was to investigate the effect of supercritical carbon dioxide (SC-CO2) treatment for the sterilization purpose on meat quality and protein denaturation of the porcine longissimus dorsi muscle. The conditions Of SC-CO2 treatment were 7.4 and 15.2 MPa at 3 1.1 degrees C for 10 min. SC-CO2 treatment had no effect on muscle pH, tenderness, and water-holding capacity (WHC). However, the samples treated at 7.4MPa had a higher lightness value (52.97 vs. 46.94, P < 0.001) and a more pronounced extent of sarcoplasmic protein denaturation (73.80 vs. 80.73, P < 0.01) than the control samples. These results suggest that the paler color of samples treated with SC-CO2 was associated with the sarcoplasmic protein denaturation, and the major denaturated proteins were determined to be phosphorylase b (PH), creatine kinase (CK), triosephophate isomerase (TPI), and one unknown protein. On the other hand, other quality traits were generally unaffected by the SC-CO2 treatments at 7.4 or 15.2MPa. (0 2007 Swiss Society of Food Science and Technology. Published by Elsevier Ltd. All rights reserved.-
dc.languageEnglish-
dc.language.isoen-
dc.publisherELSEVIER-
dc.subjectMYOSIN HEAVY-CHAIN-
dc.subjectHIGH-PRESSURE-
dc.subjectPROTEIN SOLUBILITY-
dc.subjectISOFORMS-
dc.titleEffects of supercritical carbon dioxide treatment for sterilization purpose on meat quality of porcine longissimus dorsi muscle-
dc.typeArticle-
dc.contributor.affiliatedAuthorChoi, Y. M.-
dc.contributor.affiliatedAuthorKim, K. H.-
dc.contributor.affiliatedAuthorRhee, M. S.-
dc.contributor.affiliatedAuthorKim, B. C.-
dc.identifier.doi10.1016/j.lwt.2007.02.020-
dc.identifier.scopusid2-s2.0-36048958216-
dc.identifier.wosid000251449800016-
dc.identifier.bibliographicCitationLWT-FOOD SCIENCE AND TECHNOLOGY, v.41, no.2, pp.317 - 322-
dc.relation.isPartOfLWT-FOOD SCIENCE AND TECHNOLOGY-
dc.citation.titleLWT-FOOD SCIENCE AND TECHNOLOGY-
dc.citation.volume41-
dc.citation.number2-
dc.citation.startPage317-
dc.citation.endPage322-
dc.type.rimsART-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaFood Science & Technology-
dc.relation.journalWebOfScienceCategoryFood Science & Technology-
dc.subject.keywordPlusMYOSIN HEAVY-CHAIN-
dc.subject.keywordPlusHIGH-PRESSURE-
dc.subject.keywordPlusPROTEIN SOLUBILITY-
dc.subject.keywordPlusISOFORMS-
dc.subject.keywordAuthorsupercritical carbon dioxide-
dc.subject.keywordAuthormeat quality-
dc.subject.keywordAuthorprotein denaturation-
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