دورية أكاديمية
Proteomic investigation of protein profile changes and amino acid residue-level modification in cooked lamb longissimus thoracis et lumborum: The effect of roasting
| العنوان: | Proteomic investigation of protein profile changes and amino acid residue-level modification in cooked lamb longissimus thoracis et lumborum: The effect of roasting |
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| المؤلفون: | Yu, T-Y, Morton, James, Clerens, S, Dyer, JM |
| بيانات النشر: | Elsevier on behalf of the American Meat Science Association |
| سنة النشر: | 2016 |
| المجموعة: | Lincoln University (New Zealand): Lincoln U Research Archive |
| مصطلحات موضوعية: | sheep, lamb, meat, cooking, proteomics, protein modifications, roasting, ANZSRC::090803 Food Nutritional Balance, ANZSRC::3003 Animal production, ANZSRC::3006 Food sciences, Myofibrils, Sarcoplasmic Reticulum, Animals, Phosphopyruvate Hydratase, L-Lactate Dehydrogenase, Phosphofructokinase-1, Amino Acids, Muscle Proteins, Actinin, Chromatography, Liquid, Tandem Mass Spectrometry, Hot Temperature, Paraspinal Muscles, Red Meat |
| جغرافية الموضوع: | England |
| الوصف: | Protein modifications of meat cooked by typical dry-heat methods (e.g., roasting) are currently not well understood. The present study utilised a shotgun proteomic approach to examine the molecular-level effect of roasting on thin lamb longissimus thoracis et lumborum patties, in terms of changes to both the protein profile and amino acid residue side-chain modifications. Cooking caused aggregation of actin, myosin heavy chains and sarcoplasmic proteins. Longer roasting time resulted in significantly reduced protein extractability as well as protein truncation involving particularly a number of myofibrillar and sarcoplasmic proteins, e.g., 6-phosphofructokinase, beta-enolase, l-lactate dehydrogenase A chain, alpha-actinin-3, actin and possibly myosin heavy chains. Modifications that have potential influence on nutritional properties, including carboxyethyllysine and a potentially glucose-derived N-terminal Amadori compound, were observed in actin and myoglobin after roasting. This study provided new insights into molecular changes resulting from the dry-heat treatment of meat, such as commonly used in food preparation. |
| نوع الوثيقة: | article in journal/newspaper |
| وصف الملف: | pp.80-88; Print-Electronic |
| اللغة: | English |
| تدمد: | 1873-4138 0309-1740 |
| العلاقة: | The original publication is available from Elsevier on behalf of the American Meat Science Association - https://doi.org/10.1016/j.meatsci.2016.04.024Test - http://dx.doi.org/10.1016/j.meatsci.2016.04.024Test; Meat Science; https://doi.org/10.1016/j.meatsci.2016.04.024Test; S0309-1740(16)30117-6; https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=elements_prod&SrcAuth=WosAPI&KeyUT=WOS:000378452100011&DestLinkType=FullRecord&DestApp=WOS_CPLTest; Yu, T-Y., Morton, J.D., Clerens, S., & Dyer, J.M. (2016). Proteomic investigation of protein profile changes and amino acid residue-level modification in cooked lamb longissimus thoracis et lumborum: The effect of roasting. Meat Science, 119, 80-88. doi:10.1016/j.meatsci.2016.04.024; 27150797 (pubmed); https://hdl.handle.net/10182/8518Test |
| DOI: | 10.1016/j.meatsci.2016.04.024 |
| الإتاحة: | https://doi.org/10.1016/j.meatsci.2016.04.024Test https://hdl.handle.net/10182/8518Test https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=elements_prod&SrcAuth=WosAPI&KeyUT=WOS:000378452100011&DestLinkType=FullRecord&DestApp=WOS_CPLTest |
| حقوق: | © 2016 Elsevier Ltd. All rights reserved. |
| رقم الانضمام: | edsbas.D0AD03DB |
| قاعدة البيانات: | BASE |
| تدمد: | 18734138 03091740 |
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| DOI: | 10.1016/j.meatsci.2016.04.024 |