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Discoloration Characteristics of 3 Major Muscles From Cattle During Cold Storage

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dc.contributor.authorJeong, J. Y.-
dc.contributor.authorHur, S. J.-
dc.contributor.authorYang, H. S.-
dc.contributor.authorMoon, S. H.-
dc.contributor.authorHwang, Y. H.-
dc.contributor.authorPark, G. B.-
dc.contributor.authorJoo, S. T.-
dc.date.accessioned2022-12-27T05:21:27Z-
dc.date.available2022-12-27T05:21:27Z-
dc.date.issued2009-01-
dc.identifier.issn0022-1147-
dc.identifier.issn1750-3841-
dc.identifier.urihttps://scholarworks.gnu.ac.kr/handle/sw.gnu/26443-
dc.description.abstractDiscoloration characteristics of 3 major muscles (LD, Longissimus dorsi; PM, Psoas major; SM, Semimemebranosus) from Korean native cattle (Hanwoo) were monitored during 7 d of cold storage at 4 degrees C. The muscles were obtained from 12 Hanwoo carcasses at 24 h postmortem. Meat color (CIE L*, a*, b*), myoglobin (Mb) concentration, chemical form, metmyoglobin (MetMb) reducing ability (MRA), mitochondria concentration, and thiobarbituric acid reactive substance (TBARS) were measured at 1, 3, 5, and 7 d of storage. Although there were no significant differences in CIE a* and b*-values between the 3 muscles at day 1, the values of PM muscle were significantly (P < 0.05) lower than those of LD and SM muscles at day 5 and 7. PM muscle showed a rapid decrease in the oxymyoglobin (OxyMb) and an increase in MetMb, which resulted in a significantly (P < 0.05) higher percentage of MetMb in PM muscle compared to LD and SM muscles. Also, the Mb and mitochondria concentration of PM muscle was significantly (P < 0.05) higher than those of LD and SM muscles. However, there were no significant differences in MRA, pH, or TBARS between the 3 muscles during 7 d of cold storage. It was concluded that rapid discoloration (that is, MetMb accumulation) in PM muscle of Hanwoo could be due to its higher contents of Mb and mitochondria.-
dc.language영어-
dc.language.isoENG-
dc.publisherWILEY-
dc.titleDiscoloration Characteristics of 3 Major Muscles From Cattle During Cold Storage-
dc.typeArticle-
dc.publisher.location미국-
dc.identifier.doi10.1111/j.1750-3841.2008.00983.x-
dc.identifier.wosid000262647800004-
dc.identifier.bibliographicCitationJOURNAL OF FOOD SCIENCE, v.74, no.1, pp C1 - C5-
dc.citation.titleJOURNAL OF FOOD SCIENCE-
dc.citation.volume74-
dc.citation.number1-
dc.citation.startPageC1-
dc.citation.endPageC5-
dc.type.docTypeArticle-
dc.description.isOpenAccessY-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaFood Science & Technology-
dc.relation.journalWebOfScienceCategoryFood Science & Technology-
dc.subject.keywordPlusINFLUENCING METMYOGLOBIN FORMATION-
dc.subject.keywordPlusLONGISSIMUS MUSCLE-
dc.subject.keywordPlusSKELETAL-MUSCLE-
dc.subject.keywordPlusBOVINE MUSCLES-
dc.subject.keywordPlusHEME PIGMENTS-
dc.subject.keywordPlusBEEF MUSCLES-
dc.subject.keywordPlusSTABILITY-
dc.subject.keywordPlusREDUCTASE-
dc.subject.keywordPlusMEAT-
dc.subject.keywordPlusCONSUMPTION-
dc.subject.keywordAuthordiscoloration of beef-
dc.subject.keywordAuthorhanwoo muscles-
dc.subject.keywordAuthormyoglobin oxidation-
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