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首页> 外文期刊>Food & Function >ACE inhibitory peptides derived from de-fatted lemon basil seeds: optimization, purification, identification, structure-activity relationship and molecular docking analysis
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ACE inhibitory peptides derived from de-fatted lemon basil seeds: optimization, purification, identification, structure-activity relationship and molecular docking analysis

机译：ACE抑制型肽衍生自去污柠檬罗勒种子：优化，纯化，鉴定，结构 - 活性关系和分子对接分析

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The oil processing industry generates significant quantities of lemon basil seed residue which is not currently used to any significant extent. However, this by-product has important potential as a source of bioactive peptides which may play a role as ingredients in functional foods. This study therefore sought to optimize the preparation techniques used to obtain the necessary protein hydrolysate from de-fatted lemon basil seeds (DLBS), and subsequently to examine the ACE inhibitory capabilities of the resulting hydrolysate. Response Surface Methodology (RSM) was used for the hydrolysis of DLBS by Alcalase (R), with observation of the resulting ACE inhibitory activity and degree of hydrolysis (DH). The optimum conditions were 55 degrees C and 103 minutes with a ratio of enzyme to substrate of 7.0% w/v. The hydrolysate was fractionated by ultrafiltration and purified through RP-HPLC. The results reveal that the F(2)sub-fraction demonstrated the highest ACE inhibitory activity. The amino acid sequence of this peak was identified by mass spectrometry as LGRNLPPI and GPAGPAGL with a molecular weight of 879.06 and 639.347 Dalton, respectively. These peptides were classified as non-toxic and bitter peptides. For the synthesized version of these peptides, the ACE inhibitory activity values, measured by IC50, were 0.124 +/- 0.02 mM and 0.013 +/- 0.001 mM, respectively. Analysis of the Lineweaver-Burk plot confirmed that these peptides served as non-competitive ones. The study of molecular docking showed that the ACE inhibitory behavior of both purified peptides was mainly due to the interactions of the hydrogen bonds between the peptides and ACE. It is therefore suggested that DLBS may be a useful raw material allowing the production of antihypertensive peptides which can offer therapeutic and commercial benefits as an ingredient in functional foods.
机译：石油加工业产生大量的柠檬罗勒种子残留物，目前没有任何显着程度。然而，这种副产物具有作为生物活性肽来源的重要潜力，这可能在功能性食品中发挥作用。因此，该研究寻求优化用于获得从脱脂柠檬罗勒籽（DLB）的必要蛋白水解产物的制备技术，然后检查所得水解产物的ACE抑制能力。响应表面方法（RSM）用于通过alcalase（R）的DLBs水解，观察结果的ACE抑制活性和水解度（DH）。最佳条件为55℃，103分钟，酶与底物的比例为7.0％w / v。通过超滤分离水解产物并通过RP-HPLC纯化。结果表明，F（2）次级分数显示出最高的ACE抑制活性。通过质谱法作为LGRNLPPI和HPAGPGL分别鉴定该峰的氨基酸序列，分别为879.06和639.347道尔顿。将这些肽被归类为无毒和苦肽。对于这些肽的合成版本，通过IC 50测量的ACE抑制活性值分别为0.124 +/- 0.02mm和0.013 +/- 0.001mm。对LineWeaver-Burk图的分析证实这些肽用作非竞争性的。分子对接的研究表明，纯化肽的ACE抑制行为主要是由于肽和ACE之间的氢键的相互作用。因此，表明DLB可以是一种有用的原料，允许生产可提供治疗和商业益处作为功能性食品的成分。

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  • 来源
    《Food & Function》 |2020年第9期|共18页
  • 作者

    Kheeree Norhameemee; Sangtanoo Papassara; Srimongkol Piroonporn; Saisavoey Tanatorn; Reamtong Onrapak; Choowongkomon Kiattawee; Karnchanatat Aphichart;

  • 作者单位

    Chulalongkorn Univ Fac Sci Program Biotechnol 254 Phayathai Rd Bangkok 10330 Thailand;

    Chulalongkorn Univ Inst Biotechnol &

    Genet Engn Res Unit Bioconvers Bioseparat Value Added Chem P 251 Phayathai Rd Bangkok 10330 Thailand;

    Chulalongkorn Univ Inst Biotechnol &

    Genet Engn Res Unit Bioconvers Bioseparat Value Added Chem P 251 Phayathai Rd Bangkok 10330 Thailand;

    Chulalongkorn Univ Inst Biotechnol &

    Genet Engn Res Unit Bioconvers Bioseparat Value Added Chem P 251 Phayathai Rd Bangkok 10330 Thailand;

    Mahidol Univ Fac Trop Med Dept Mol Trop Med &

    Genet 420-6 Ratchawithi Rd Bangkok 10400 Thailand;

    Kasetsart Univ Fac Sci Dept Biochem Bangkok 10903 Thailand;

    Chulalongkorn Univ Inst Biotechnol &

    Genet Engn Res Unit Bioconvers Bioseparat Value Added Chem P 251 Phayathai Rd Bangkok 10330 Thailand;

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