Changes in Zn-porphyrin and proteinous pigments in italian dry-cured ham during processing and maturation
Changes in Zn-porphyrin and proteinous pigments in italian dry-cured ham during processing and maturation
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DOI：
10.1016/j.meatsci.2006.04.003
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发表时间：
2006-10-01
期刊：
影响因子：
7.1
通讯作者：
Skibsted, Leif H.
中科院分区：
文献类型：
--
作者：
Adamsen, Christina E.;Moller, Jens K. S.;Skibsted, Leif H.
研究发现，在帕尔马火腿成熟过程中，肌红蛋白中的铁被锌取代，产生卟啉锌，可通过75%体积/体积的丙酮/水溶液提取，并可通过荧光光谱检测，这与肌红蛋白中的蛋白质修饰同时发生。在帕尔马火腿的整个加工和成熟过程中，卟啉锌的含量都在增加，从青火腿的I-fl 0.1 +/- 0.06到完全成熟的帕尔马火腿的I-fl 84.4 +/- 48.8。在pH值为6.0的帕尔马火腿的水萃取物中，通过尺寸排除色谱法检测到肌红蛋白的变化是在盐腌后的静息期开始的，似乎先于卟啉锌的形成。结果表明，在成熟过程中，修饰的肌红蛋白可以发生聚合，并且表明初始的蛋白质变性或降解有助于铁与锌的取代。色素聚合可能是变性或部分降解肌红蛋白中非共价蛋白与卟啉锌结合的结果。(c) 2006 Elsevier Ltd.版权所有。
Substitution of iron with zinc in myoglobin during maturation of Parma ham to yield zinc porphyrin extractable by 75% vol/vol acetone/water solution and detectable by fluorescence spectroscopy, was found to occur concomitant with protein modification in myoglobin. The content of zinc porphyrin increases throughout the whole processing and maturation of Parma ham, from I-fl 0.1 +/- 0.06 for green ham to I-fl 84.4 +/- 48.8 for fully matured Parma ham. In an aqueous extract of Parma ham with pH 6.0 protein alteration in myoglobin, as detected by size-exclusion chromatography, is initiated during the resting period following salting and seems to precede formation of zinc porphyrin. During maturation the results indicate that the modified myoglobin could undergo polymerization, and it is suggested that initial protein denaturation or degradation facilitates substitution of iron with zinc. The pigment polymerization may be a result of non-covalent protein association to zinc porphyrin in denatured or partly degraded myoglobin. (c) 2006 Elsevier Ltd. All rights reserved.