| Decreased gelling and emulsifying properties of myofibrillar protein from repeatedly frozen-thawed porcine longissimus muscle are due to protein denaturation and susceptibility to aggregation. | |
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MedLine Citation:
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PMID: 20416818 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The effects of freeze-thaw cycles (FT, 0, 1, 3 and 5 times) on protein functional properties of porcine longissimus muscle were investigated. FT increased gapping between muscle fibres and tore muscle fiber bundles. Myofibrillar protein (MP) isolated from FT muscle showed an increased hydrophobicity (P<0.05), reduced thermal transition temperatures (T(max)) and enthalpy of denaturation (DeltaH) (P<0.05), and enhanced susceptibility to thermal aggregation. These structural changes resulted in major losses in protein functionalities, e.g., 41-43% reductions (P<0.05) in MP emulsifying capacity and emulsion stability after five FT cycles. The ability of MP to form a viscoelastic gel network, as analyzed by small-strain oscillatory rheological testing, also attenuated with FT cycles. The FT process lowered (P<0.05) water-holding capacity (WHC), whiteness, and texture (hardness, springiness, chewiness and cohesiveness) of MP gels. Overall, repeated FT had a detrimental effect on the general functionality of porcine MP, and protein denaturation and aggregation were implicated in the functionality losses. |
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Authors:
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Xiufang Xia; Baohua Kong; Youling Xiong; Yanming Ren |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2010-02-20 |
Journal Detail:
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Title: Meat science Volume: 85 ISSN: 1873-4138 ISO Abbreviation: Meat Sci. Publication Date: 2010 Jul |
Date Detail:
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Created Date: 2010-05-07 Completed Date: 2010-11-23 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101160862 Medline TA: Meat Sci Country: England |
Other Details:
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Languages: eng Pagination: 481-6 Citation Subset: IM |
Copyright Information:
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Copyright 2010 Elsevier Ltd. All rights reserved. |
Affiliation:
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College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Dietary Proteins* Emulsions Food Handling* Freezing* Gels Hydrophobic and Hydrophilic Interactions Meat / standards* Muscle Proteins / chemistry* Muscle, Skeletal / chemistry* Protein Denaturation Swine Temperature |
| Chemical | |
Reg. No./Substance:
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0/Dietary Proteins; 0/Emulsions; 0/Gels; 0/Muscle Proteins |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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