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首页> 外文期刊>Proteome science >Proteomic based approach for characterizing 4-hydroxy-2-nonenal induced oxidation of buffalo ( Bubalus bubalis ) and goat ( Capra hircus ) meat myoglobins
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Proteomic based approach for characterizing 4-hydroxy-2-nonenal induced oxidation of buffalo ( Bubalus bubalis ) and goat ( Capra hircus ) meat myoglobins

机译：基于蛋白质组学的方法表征4-羟基-2-壬烯诱导的水牛（Bubalus bubalis）和山羊（Capra hircus）肉类肌球蛋白的氧化

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Background Myoglobin (Mb) is a sarcoplasmic heme protein primarily responsible for meat color and its chemistry is species specific. 4-hydroxy-2-nonenal (HNE) is a cytotoxic lipid derived aldehyde detected in meat and was reported to covalently adduct with nucleophilic histidine residues of Mb and predispose it to greater oxidation. However, no literature is available on characterization of lipid oxidation induced oxidation of Indian water buffalo ( Bubalus bubalis ) and goat ( Capra hircus ) myoglobins. Methods Present study characterize the Mb extracted from water buffalo and goat cardiac muscles using two-dimensional gel electrophoresis (2DE), OFFGEL electrophoresis and mass spectrometry (MS). Purified buffalo and goat bright red oxymyoglobin were reacted with HNE in-vitro at physiological pH (7.4) and temperature (37?°C) conditions and the formation of oxidised brown metmyoglobin was measured. The Mb-HNE adducts were detected using MALDI-TOF MS, whereas specific sites of adduction was determined using ESI-QTOF MS/MS. Results Purified buffalo and goat Mb samples revealed a molecular mass of 17,043.6 and 16,899.9 Daltons, respectively. The 2DE analysis exhibited 65 (sarcoplasmic protein extract) and 6 (pure Mb) differentially expressed ( P ?0.05) protein spots between buffalo and goat samples. OFFGEL electrophoresis revealed an isoelectric point of 6.77 and 7.35 respectively, for buffalo and goat Mb’s. In-vitro incubation of HNE with bright red buffalo and goat oxymyoglobin’s at pH?7.4 and 37?°C resulted in pronounced ( P ?0.05) oxidation and formation of brown metmyoglobin. MALDI-TOF MS analysis of Mb-HNE reaction mix revealed covalent binding (via Michael addition) of 3 and 5 molecules of HNE with buffalo and goat Oxy-Mb’s, respectively. ESI-QTOF MS/MS identified seven and nine histidine (HIS) residues of Mb that were readily adducted by HNE in buffalo and goat, respectively. Conclusion The study demonstrated better redox stability of buffalo Mb than goat Mb. Our findings confirm the hypothesis that relative effect of HNE was greater for Mb’s with 12?±?1 HIS residues than Mb’s with 9 HIS residues and helps meat processors in developing species-specific processing strategies to reduce the color variability.
机译：背景肌红蛋白（Mb）是肌浆血红素蛋白，主要负责肉色，其化学性质是物种特异性的。 4-羟基-2-壬烯醛（HNE）是一种在肉中检测到的细胞毒性脂质衍生的醛，据报道与Mb的亲核组氨酸残基共价加成，并易于氧化。然而，关于脂质氧化诱导的印度水牛（Bubalus bubalis）和山羊（Capra hircus）肌球蛋白氧化的表征尚无相关文献。方法本研究利用二维凝胶电泳（2DE），OFFGEL电泳和质谱（MS）表征从水牛和山羊心肌中提取的Mb。在生理pH（7.4）和温度（37°C）条件下，将纯化的水牛和山羊鲜红色的氧肌红蛋白与HNE进行体外反应，并测量氧化的棕色肌红蛋白的形成。使用MALDI-TOF MS检测Mb-HNE加合物，而使用ESI-QTOF MS / MS确定加合物的特定位点。结果纯化的水牛和山羊Mb样品的分子量分别为17,043.6和16,899.9道尔顿。 2DE分析显示在水牛和山羊样品之间有65个（肌浆蛋白提取物）和6个（纯Mb）差异表达的蛋白点（P <？0.05）。 OFFGEL电泳显示，水牛和山羊Mb's的等电点分别为6.77和7.35。 HNE与鲜红色的水牛和山羊含氧肌红蛋白在pH？7.4和37？C下的体外温育导致（P <？0.05）明显的氧化并形成棕色的肌红蛋白。 Mb-HNE反应混合物的MALDI-TOF MS分析表明，3和5个分子的HNE与水牛和山羊Oxy-Mb共价结合（通过迈克尔加成法）。 ESI-QTOF MS / MS鉴定了水牛和山羊中HNE容易加成的Mb的七个和九个组氨酸（HIS）残基。结论该研究表明水牛Mb的氧化还原稳定性优于山羊Mb。我们的发现证实了这样的假设，即HNE对具有12？±？1 HIS残留的Mb的相对作用要大于对具有9 HIS残留的Mb的相对作用，并有助于肉类加工者制定针对特定物种的加工策略以减少颜色变异性。

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