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首页> 外文期刊>Meat Science >Assessment of the angiotensin-I-converting enzyme (ACE-I) inhibitory and antioxidant activities of hydrolysates of bovine brisket sarcoplasmic proteins produced by papain and characterisation of associated bioactive peptidic fractions
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Assessment of the angiotensin-I-converting enzyme (ACE-I) inhibitory and antioxidant activities of hydrolysates of bovine brisket sarcoplasmic proteins produced by papain and characterisation of associated bioactive peptidic fractions

机译:评估木瓜蛋白酶产生的牛胸肉质蛋白水解产物的血管紧张素转换酶(ACE-I)抑制和抗氧化活性及相关生物活性肽组分的表征

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摘要

The main objective was to investigate the angiotensin-I-converting enzyme (ACE-I) inhibitory and antioxidant activities of sarcoplasmic proteins isolated from the brisket muscle (Pectoralis profundus) of 3 (Bos taunts) cattle and hydrolysed with papain for 24 h at 37 ℃. Sarcoplasmic protein hydrolysates were ultra-filtered using molecular weight cut off (MWCO) membranes and 10-kDa and 3-kDa filtrates were obtained. The total sarcoplasmic protein extracts and the 3-kDa filtrates were tested for angiotensin I-converting enzyme inhibitory (ACE-I) activities. The total hydrolysates, 10-kDa and 3-kDa filtrates were also tested for their associated antioxidant activities using the 2,2-diphenyl-l-picrylhydrazyl (DPPH) radical scavenging activity assay, the ferric ion reducing antioxidant power (FRAP) assay and the Fe~(2+) metal chelating ability assay. The peptidic content of the total hydrolysates, the 10-kDa and the 3-kDa filtrates were analysed using an ORBITRAP mass spectrometer, and mass spectral data obtained were analysed using TurboSEQUEST. Eleven peptides were characterised from the total hydrolysates, fifteen from the 10-kDa filtrate fractions, whilst nine peptides were characterised from the 3-kDa filtrate fractions. Similarities between the amino acid sequences of the peptides identified in this study and previously identified antioxidant and ACE-I inhibitory peptides detailed in the BIOPEP database were outlined.
机译:主要目的是研究从3头牛(Bos taunt牛)的牛the肌(胸大肌)分离的肌浆蛋白的血管紧张素-I转换酶(ACE-I)的抑制和抗氧化活性,并在37℃下用木瓜蛋白酶水解24 h ℃。使用截留分子量(MWCO)膜对肌浆蛋白水解物进行超滤,得到10-kDa和3-kDa滤液。测试了总的肌浆蛋白提取物和3-kDa滤液的血管紧张素I转化酶抑制(ACE-I)活性。还使用2,2-二苯基-1-吡啶甲基肼基(DPPH)自由基清除活性测定法,三价铁离子还原抗氧化剂能力(FRAP)测定法和10kDa和3kDa滤液总水解物的相关抗氧化活性。 Fe〜(2+)金属螯合能力的测定。使用ORBITRAP质谱仪分析总水解产物,10 kDa和3 kDa滤液的肽含量,并使用TurboSEQUEST分析获得的质谱数据。从总水解物中鉴定出11种肽,从10 kDa滤液组分中鉴定出15种肽,而从3 kDa滤液组分中鉴定出9种肽。概述了在这项研究中鉴定的肽的氨基酸序列与BIOPEP数据库中详述的先前鉴定的抗氧化剂和ACE-1抑制肽之间的相似性。

著录项

  • 来源
    《Meat Science》 |2012年第1期|p.226-235|共10页
  • 作者单位

    Food Chemistry and Technology Department, Teagasc Food Research Centre, Ashtown, Dublin 15, Ireland;

    Food Chemistry and Technology Department, Teagasc Food Research Centre, Ashtown, Dublin 15, Ireland;

    Department of Food Safety, Teagasc Food Research Centre, Ashtown, Dublin 15, Ireland;

    School of Food and Nutritional Sciences, University College Cork, Cork, Ireland;

    School of Food and Nutritional Sciences, University College Cork, Cork, Ireland;

    Food Biosciences Department, Teagasc Food Research Centre, Ashtown, Dublin 15, Ireland;

  • 收录信息 美国《科学引文索引》(SCI);
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

    antioxidant peptides; bovine meat; papain; hydrolysis; brisket muscle; ACE-1 inhibitory peptides;

    机译:抗氧化剂肽牛肉木瓜蛋白酶水解;胸肌ACE-1抑制肽;

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