{"refrec":{"BRefID":293786,"RR":"<b>Verhaeghe, T.; Vlaemynck, G.; De Block, J.; Van Weyenberg, S.; Braeckman, R.; Hendrickx, M.E.</b> (2016). Kinetics of heat induced muscle protein denaturation of brown shrimp (<i>Crangon crangon</i>). <i>Journal of Food Engineering 191</i>: 88-94. <a href=\"https://dx.doi.org/10.1016/j.jfoodeng.2016.07.010\" target=\"_blank\">https://dx.doi.org/10.1016/j.jfoodeng.2016.07.010</a>","BEntID":285850,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>Journal of Food Engineering 191</i>: 88-94. <a href=\"https://dx.doi.org/10.1016/j.jfoodeng.2016.07.010\" target=\"_blank\">https://dx.doi.org/10.1016/j.jfoodeng.2016.07.010</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Verhaeghe, T.; Vlaemynck, G.; De Block, J.; Van Weyenberg, S.; Braeckman, R.; Hendrickx, M.E.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Verhaeghe, T. <i>et al.</i>","Englishabstract":"To optimize the quality of cooked brown shrimp (<i>Crangon crangon</i>), quantitative data on the influence of all relevant process parameters (treatment time, temperature, NaCl concentration) on several quality attributes are required. Surprisingly, kinetic data and models on heat induced quality changes of brown shrimp are scarce. In this study, the denaturation of muscle proteins was studied by differential scanning calorimetry. The thermal denaturation kinetics of actin, the most heat resistant muscle protein, were determined and showed a first order decay with <i>k</i><sub>72 °C</sub> = 0.038 ± 0.001 min<sup>−1</sup> and <i>Ea</i> = 388 ± 7.3 kJ/mol. Spiking experiments showed that NaCl (concentrations in the range from 1 to 5% NaCl) had a negligible influence on the actin thermal stability. The kinetic data obtained can be used to quantitatively evaluate the doneness of cooked shrimp.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Kinetics of heat induced muscle protein denaturation of brown shrimp (<i>Crangon crangon</i>)","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2024-12-10 01:33:17.368041","timezone_type":1,"timezone":"+01:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":"Crangon crangon; Muscle protein denaturation; Actin; Thermal stability;Kinetics","OtherDescriptors":null,"Notes":null,"AnaPub":2016,"MonPub":null,"DateUpdate":"2022-07-13","DateCreate":"2018-03-12","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000383297500010","VABBcode":null,"OpenAcc":0,"DOI":"10.1016/j.jfoodeng.2016.07.010"},"refs":null,"anarec":{"AnaID":293786,"PubliDate":2016,"Pagination":"88-94","XtraPublOfAnaID":null,"ISBN":null,"Volume":"191","Issue":null,"BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":272031,"SerRR":"Journal of Food Engineering. 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