Mostrar el registro sencillo del ítem
dc.contributor.author | Wang, Zhaoming | es_ES |
dc.contributor.author | He, Z. | es_ES |
dc.contributor.author | Gan, X. | es_ES |
dc.contributor.author | Li, Hongjun | es_ES |
dc.date.accessioned | 2018-07-03T06:52:29Z | |
dc.date.available | 2018-07-03T06:52:29Z | |
dc.date.issued | 2018-06-28 | |
dc.identifier.issn | 1257-5011 | |
dc.identifier.uri | http://hdl.handle.net/10251/105085 | |
dc.description.abstract | [EN] We investigated the effect of repeated freeze-thaw cycles on the quality of rabbit meat. Twenty-five Hyla rabbits were slaughtered using standard commercial procedures. A freeze-thaw procedure—i.e., seven days frozen at –18°C followed by thawing at 4°C for 12h— was repeated 5 times, and 9 Longissimus thoracis et lumborum muscles were randomly selected at pre-set cycles (0, 1, 2, 3, and 5). The Longissimus lumborum muscles were used to determine meat quality parameters, while the Longissimus thoracis muscles were used for chemical analysis. During the repeated freeze-thaw process, muscle pH, redness, hardness, and water holding capacity gradually decreased, whereas meat lightness and yellowness gradually increased. The amount of total volatile basic nitrogen significantly increased (P<0.05) and exceeded the threshold value for frozen meat after 5 repeated freeze-thaw cycles. The metmyoglobin proportion, thiobarbituric acid-reactive substances (TBARS) and protein carbonyl content in rabbit meat samples increased with a higher number of freeze-thaw cycles (P<0.05), and the proportions of these compounds were positively correlated. During the repeated freeze-thaw process, extractable haeme iron levels significantly decreased (P<0.05), and non-haeme iron levels markedly increased (P<0.05). An sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis indicated that the degradation of both water- and salt-soluble proteins was more prevalent in samples subjected to higher numbers of freeze-thaw cycles. Additionally, a principal component analysis identified good correlations between physicochemical properties (TBARS, protein carbonyl levels and metmyoglobin content) and quality parameters (thawing loss, redness, lightness and hardness). Taken together, we conclude that the repeated freeze-thaw process can strongly affect rabbit meat quality as well as its physicochemical properties. | es_ES |
dc.description.sponsorship | The authors gratefully acknowledge financial support from the General Program of National Natural Science Foundation of China (31671787), the National Rabbit Industry Technology System Programme (Grant No. CARS-43-E-1), and the Chongqing Herbivorous Livestock Industry Technology System (Y201706). | es_ES |
dc.language | Inglés | es_ES |
dc.publisher | Universitat Politècnica de València | |
dc.relation.ispartof | World Rabbit Science | |
dc.rights | Reserva de todos los derechos | es_ES |
dc.subject | Rabbit | es_ES |
dc.subject | Freeze-thaw cycles | es_ES |
dc.subject | Meat quality | es_ES |
dc.subject | Myoglobin oxidation | es_ES |
dc.subject | Lipid oxidation | es_ES |
dc.subject | Protein oxidation | es_ES |
dc.title | The effect of repeated freeze-thaw cycles on the meat quality of rabbit | es_ES |
dc.type | Artículo | es_ES |
dc.date.updated | 2018-06-29T09:57:30Z | |
dc.identifier.doi | 10.4995/wrs.2018.8616 | |
dc.relation.projectID | info:eu-repo/grantAgreement/NSFC//31671787/ | |
dc.relation.projectID | info:eu-repo/grantAgreement/Chongqing Herbivorous Livestock Industry Technology System//Y201706/ | |
dc.relation.projectID | info:eu-repo/grantAgreement/Earmarked Fund for Modern Agro-industry Technology Research System, China//CARS-43-E-1/ | |
dc.rights.accessRights | Abierto | es_ES |
dc.description.bibliographicCitation | Wang, Z.; He, Z.; Gan, X.; Li, H. (2018). The effect of repeated freeze-thaw cycles on the meat quality of rabbit. World Rabbit Science. 26(2):165-177. https://doi.org/10.4995/wrs.2018.8616 | es_ES |
dc.description.accrualMethod | SWORD | es_ES |
dc.relation.publisherversion | https://doi.org/10.4995/wrs.2018.8616 | es_ES |
dc.description.upvformatpinicio | 165 | es_ES |
dc.description.upvformatpfin | 177 | es_ES |
dc.type.version | info:eu-repo/semantics/publishedVersion | es_ES |
dc.description.volume | 26 | |
dc.description.issue | 2 | |
dc.identifier.eissn | 1989-8886 | |
dc.contributor.funder | National Natural Science Foundation of China | |
dc.contributor.funder | Earmarked Fund for Modern Agro-industry Technology Research System, China | |
dc.contributor.funder | Chongqing Herbivorous Livestock Industry Technology System | |
dc.description.references | Ali S., Rajput N., Li C.B., Zhang W., Zhou G.H. 2016. Effect of freeze-thaw cycles on lipid oxidation and myowater in broiler chickens. Revista Brasileira de Ciência Avícola, 18: 35-40. | es_ES |
dc.description.references | https://doi.org/10.1590/1516-635x1801035-040 | es_ES |
dc.description.references | Ali S., Zhang W., Rajput N., Khan M.A., Li C.B., Zhou G.H. 2015. Effect of multiple freeze-thaw cycles on the quality of chicken breast meat. Food Chem., 173: 808-814. https://doi.org/10.1016/j.foodchem.2014.09.095 | es_ES |
dc.description.references | Alonso V., Muela E., Tenas J., Calanche J.B., Roncalés P., Beltrán J.A. 2016. Changes in physicochemical properties and fatty acid composition of pork following long-term frozen storage. Eur. Food Res. Technol., 242: 2119-2127. https://doi.org/10.1007/s00217-016-2708-y | es_ES |
dc.description.references | Barbin D.F., Sun D.W., Su C. 2013. NIR hyperspectral imaging as non-destructive evaluation tool for the recognition of fresh and frozen-thawed porcine longissimus dorsi muscles. Innov. Food Sci. Emerg., 18: 226-236. https://doi.org/10.1016/j.ifset.2012.12.011 | es_ES |
dc.description.references | Benjakul S., Bauer F. 2001. Biochemical and physicochemical changes in catfish (Silurus glanis Linne) muscle as influenced by different freeze-thaw cycles. Food Chem., 72: 207-217. | es_ES |
dc.description.references | https://doi.org/10.1016/S0308-8146(00)00222-3 | es_ES |
dc.description.references | Berardo A., Claeys E., Vossen E., Leroy F., De Smet S. 2015. Protein oxidation affects proteolysis in a meat model system. Meat Sci., 10: 78-84. https://doi.org/10.1016/j.meatsci.2015.04.002 | es_ES |
dc.description.references | Bianchi M., Petracci M., Cavani C. 2006. Effects of dietary inclusion of dehydrated lucerne and whole linseed on rabbit meat quality. World Rabbit Sci., 14: 247-258. https://doi.org/10.4995/wrs.2006.562 | es_ES |
dc.description.references | Cai J., Chen Q., Wan X., Zhao J. 2011. Determination of total volatile basic nitrogen (TVB-N) content and Warner-Bratzler shear force (WBSF) in pork using Fourier transform near infrared (FT-NIR) spectroscopy. Food Chem., 126: 1354-1360. https://doi.org/10.1016/j.foodchem.2010.11.098 | es_ES |
dc.description.references | Chen Q., Zhang Y., Zhao J., Hui Z. 2013. Nondestructive measurement of total volatile basic nitrogen (TVB-N) content in salted pork in jelly using a hyperspectral imaging technique combined with efficient hypercube processing algorithms. Anal. Methods-UK, 5: 6382-6388. https://doi.org/10.1039/C3AY40436F | es_ES |
dc.description.references | Chen T.H., Zhu Y.P., Han M.Y., Wang P., Wei R., Xu X.L., Zhou G.H. 2017. Classification of chicken muscle with different freeze-thaw cycles using impedance and physicochemical properties. J. Food Eng., 196: 94-100. https://doi.org/10.1016/j.jfoodeng.2016.10.003 | es_ES |
dc.description.references | Dai Y., Miao J., Yuan S.Z., Liu Y., Li X.M., Dai R.T. 2013. Colour and sarcoplasmic protein evaluation of pork following water bath and ohmic cooking. Meat Sci., 93: 898-905. https://doi.org/10.1016/j.meatsci.2012.11.044 | es_ES |
dc.description.references | Dai Y., Lu Y., Wu W., Lu X.M., Han Z.P., Liu Y., Li X.M., Dai R.T. 2014. Changes in oxidation, color and texture deteriorations during refrigerated storage of ohmically and water bathcooked pork meat. Innov. Food Sci. Emerg., 26: 341-346. https://doi.org/10.1016/j.ifset.2014.06.009 | es_ES |
dc.description.references | Dalle Zotte A., Szendrő Z. 2011. The role of rabbit meat as functional food. Meat Sci., 88: 319-331. https://doi.org/10.1016/j.meatsci.2011.02.017 | es_ES |
dc.description.references | Dalle Zotte A., Cullere M., Rémignon H., Alberghini L., Paci G. 2016. Meat physical quality and muscle fiber properties of rabbit meat as affected by the sire breed, season, parity order and gender in an organic production system. World Rabbit Sci., 24: 145-154. https://doi.org/10.4995/wrs.2016.4300 | es_ES |
dc.description.references | Dalvi-Isfahan M., Hamdami N., Le-Bail A. 2016. Effect of freezing under electrostatic field on the quality of lamb meat. Innov. Food Sci. Emerg., 37: 68-73. https://doi.org/10.1016/j.ifset.2016.07.028 | es_ES |
dc.description.references | Duun A.S., Rustad T. 2008. Quality of superchilled vacuum packed Atlantic salmon (Salmo salar) fillets stored at -1.4 and -3.6°C. Food Chem., 106: 122-131. https://doi.org/10.1016/j.foodchem.2007.05.051 | es_ES |
dc.description.references | Farouk M.M., Wieliczko K.J., Merts I. 2004. Ultra-fast freezing and low storage temperatures are not necessary to maintain the functional properties of manufacturing beef. Meat Sci., 66: 171-179. | es_ES |
dc.description.references | https://doi.org/10.1016/S0309-1740(03)00081-0 | es_ES |
dc.description.references | Hazell T. 1982. Iron and zinc compounds in the muscle meats of beef, lamb, pork and chicken. J. Sci. Food Agr., 33: 1049-1056. https://doi.org/10.1002/jsfa.2740331017 | es_ES |
dc.description.references | Huang L., Liu Q., Xia X., Kong B., Xiong Y.L. 2015. Oxidative changes and weakened gelling ability of salt-extracted protein are responsible for textural losses in dumpling meat fillings during frozen storage. Food Chem., 185: 459-469. https://doi.org/10.1016/j.foodchem.2015.04.025 | es_ES |
dc.description.references | Isleroglu H., Kemerli T., Kaymak-Ertekin F. 2015. Effect of steam-assisted hybrid cooking on textural quality characteristics, cooking loss, and free moisture content of beef. Int. J. Food Prop., 18: 403-414. https://doi.org/10.1080/10942912.2013.833219 | es_ES |
dc.description.references | Karpińska-Tymoszczyk M. 2014. The effect of antioxidants, packaging type and frozen storage time on the quality of cooked turkey meatballs. Food Chem., 148: 276-283. https://doi.org/10.1016/j.foodchem.2013.10.054 | es_ES |
dc.description.references | Kim H.W., Miller D.K., Yan F., Wang W., Cheng H.W., Kim Y.H.B. 2017. Probiotic supplementation and fast freezing to improve quality attributes and oxidation stability of frozen chicken breast muscle. LWT-Food Sci. Technol., 75: 34-41. https://doi.org/10.1016/j.lwt.2016.08.035 | es_ES |
dc.description.references | Jeong J.Y., Kim G.D., Yang H.S., Joo S.T. 2011. Effect of freezethaw cycles on physicochemical properties and color stability of beef semimembranosus muscle. Food Res. Int., 44: 3222-3228. https://doi.org/10.1016/j.foodres.2011.08.023 | es_ES |
dc.description.references | Lan Y., Shang Y., Song Y., Dong Q. 2016. Changes in the quality of superchilled rabbit meat stored at different temperatures. Meat Sci., 117: 173-181. https://doi.org/10.1016/j.meatsci.2016.02.017 | es_ES |
dc.description.references | Leygonie C., Britz T.J., Hoffman L.C. 2012. Impact of freezing and thawing on the quality of meat. Meat Sci., 91: 93-98. https://doi.org/10.1016/j.meatsci.2012.01.013 | es_ES |
dc.description.references | Maqsood S., Benjakul S. 2010. Preventive effect of tannic acid in combination with modified atmospheric packaging on the quality losses of the refrigerated ground beef. Food Control, 21: 1282-1290. https://doi.org/10.1016/j.foodcont.2010.02.018 | es_ES |
dc.description.references | Maqsood S., Benjakul S., Balange A.K. 2012. Effect of tannic acid and kiam wood extract on lipid oxidation and textural properties of fish emulsion sausages during refrigerated storage. Food Chem., 130: 408-416. https://doi.org/10.1016/j.foodchem.2011.07.065 | es_ES |
dc.description.references | Marino R., Albenzio M., Della Malva A., Caroprese M., Santillo A., Sevi A. 2014. Changes in meat quality traits and sarcoplasmic proteins during aging in three different cattle breeds. Meat Sci., 98: 178-186. https://doi.org/10.1016/j.meatsci.2014.05.024 | es_ES |
dc.description.references | Muela E., Monge P., Sañudo C., Campo M.M., Beltrán J.A. 2015. Meat quality of lamb frozen stored up to 21months: Instrumental analyses on thawed meat during display. Meat Sci., 102: 35-40. https://doi.org/10.1016/j.meatsci.2014.12.003 | es_ES |
dc.description.references | Oueslati K., de La Pomélie D., Santé-Lhoutellier V., Gatellier P. 2016. Impact of the Fenton process in meat digestion as assessed using an in vitro gastro-intestinal model. Food Chem., 209: 43-49. https://doi.org/10.1016/j.foodchem.2016.04.041 | es_ES |
dc.description.references | Qi J., Li C., Chen, Y., Gao F., Xu X., Zhou G. 2012. Changes in meat quality of ovine longissimus dorsi muscle in response to repeated freeze and thaw. Meat Sci., 92: 619-626. https://doi.org/10.1016/j.meatsci.2012.06.009 | es_ES |
dc.description.references | Rahman M.H., Hossain M.M., Rahman S.M.E., Amin M.R., Oh D.H. 2015. Evaluation of physicochemical deterioration and lipid oxidation of beef muscle affected by freezethaw cycles. Korean J. Food Sci. An., 35: 772-782. https://doi.org/10.5851/kosfa.2015.35.6.772 | es_ES |
dc.description.references | Soglia F., Petracci M., Ertbjerg P. 2016. Novel DNPH-based method for determination of protein carbonylation in muscle and meat. Food Chem., 197: 670-675. https://doi.org/10.1016/j.foodchem.2015.11.038 | es_ES |
dc.description.references | Suman S.P., Joseph P. 2013. Myoglobin chemistry and meat color. Ann. Rev. Food Sci. Tech., 4: 79-99. | es_ES |
dc.description.references | https://doi.org/10.1146/annurev-food-030212-182623 | es_ES |
dc.description.references | Tang J., Faustman C., Hoagland T.A. 2004. Krzywicki revisited: Equations for spectrophotometric determination of myoglobin redox forms in aqueous meat extracts. J. Food Sci., 69: 717-720. https://doi.org/10.1111/j.1365-2621.2004.tb09922.x | es_ES |
dc.description.references | Thanonkaew A., Benjakul S., Visessanguan W., Decker E.A. 2006. The effect of metal ions on lipid oxidation, colour and physicochemical properties of cuttlefish (Sepia pharaonis) subjected to multiple freeze-thaw cycles. Food Chem., 95: 591-599. https://doi.org/10.1016/j.foodchem.2005.01.040 | es_ES |
dc.description.references | Turhan S., Ustun N.S., Bank I. 2006. Effect of freeze-thaw cycles on total and haeme iron contents of bonito (Sarda sarda) and bluefish (Pomatomus saltator) fillets. J. Food Compos. Anal., 19: 384-387. https://doi.org/10.1016/j.jfca.2004.10.005 | es_ES |
dc.description.references | Utrera M., Morcuende D., Estévez M. 2014. Temperature of frozen storage affects the nature and consequences of protein oxidation in beef patties. Meat Sci., 96: 1250-1257. https://doi.org/10.1016/j.meatsci.2013.10.032 | es_ES |
dc.description.references | Vieira C., Diaz M. T., Martínez B., García-Cachán M.D. 2009. Effect of frozen storage conditions (temperature and length of storage) on microbiological and sensory quality of rustic crossbred beef at different states of ageing. Meat Sci., 83: 398-404. https://doi.org/10.1016/j.meatsci.2009.06.013 | es_ES |
dc.description.references | Wang H., Luo Y., Shi C., Shen H. 2015. Effect of different thawing methods and multiple freeze-thaw cycles on the quality of common carp (Cyprinus carpio). J. Aquat. Food Prod. T., 24: 153-162. https://doi.org/10.1080/10498850.2013.763884 | es_ES |
dc.description.references | Wongwichian C., Klomklao S., Panpipat W., Benjakul S., Chaijan M. 2015. Interrelationship between myoglobin and lipid oxidations in oxeye scad (Selar boops) muscle during iced storage. Food Chem., 174: 279-285. https://doi.org/10.1016/j.foodchem.2014.11.071 | es_ES |
dc.description.references | Xia X., Kong B., Liu Q., Liu J. 2009. Physicochemical change and protein oxidation in porcine longissimus dorsi as influenced by different freeze-thaw cycles. Meat Sci., 83: 239-245. https://doi.org/10.1016/j.meatsci.2009.05.003 | es_ES |
dc.description.references | Xia X., Kong B., Xiong Y., Ren Y. 2010. Decreased gelling and emulsifying properties of myofibrillar protein from repeatedly frozen-thawed porcine longissimus muscle are due to protein denaturation and susceptibility to aggregation. Meat Sci., 85: 481-486. https://doi.org/10.1016/j.meatsci.2010.02.019 | es_ES |
dc.description.references | Xie Y., He Z., Lv J., Zhang E., Li H. 2016. Identification the key odorants in different parts of Hyla rabbit meat via solid phase microextraction using gas chromatography mass spectrometry. Korean J. Food Sci. An., 36: 719-728. https://doi.org/10.5851/kosfa.2016.36.6.719 | es_ES |
dc.description.references | Yang Q., Sun D.W., Cheng W. 2017. Development of simplified models for nondestructive hyperspectral imaging monitoring of TVB-N contents in cured meat during drying process. J. Food Eng., 192: 53-60. https://doi.org/10.1016/j.jfoodeng.2016.07.015 | es_ES |