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<p>The green microalga <i>Chlamydomonas reinhardtii</i> has been approved as a new food resource. The focus of this study was to try various methods for extracting <i>Chlamydomonas reinhardtii</i> protein and use various proteases for preparing monoamine oxidase (MAO-A) inhibitory peptides. The results demonstrated that a combination of swelling, ultrasound and alkaline dissolution was found to be the best extraction method with a protein extraction percentage of 82.29%; The alkaline protease hydrolysate (APH) possessed the best MAO-A inhibitory activity with the IC<sub>50</sub> of 3.437&#xa0;mg&#xa0;mL<sup>−1</sup>, and the inhibitory activity of the ultrafiltrated fraction APH-III (&lt; 3&#xa0;kDa) can reach 73.22 ± 1.31% at 6&#xa0;mg&#xa0;mL<sup>−1</sup>. Then, 14 peptides were identified from APH-III by LC–MS/MS. Molecular docking indicated that the top high-binding peptides TEGKIPFWEGQ and GVKYGLHEVDEGATKIVQYL may interacted with MAO-A through some hydrogen bonds and hydrophobic forces. In conclusion, <i>C. reinhardtii</i>-derived protein could be potential source of bioactive peptides with inhibitory effects on depression-related enzyme MAO-A.</p>

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Extraction and hydrolysis of Chlamydomonas reinhardtii protein and in vitro MAO-A inhibitory activity of hydrolysates

  • 期刊论文

  • 发表日期：

    2025年5月13日

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  • Ya Mao,
  • Meiting Liu,
  • Keying Su,
  • Jintao Xie,
  • Wenxia Liu,
  • Lixia Wu,
  • Xuewu Zhang

摘要

The green microalga Chlamydomonas reinhardtii has been approved as a new food resource. The focus of this study was to try various methods for extracting Chlamydomonas reinhardtii protein and use various proteases for preparing monoamine oxidase (MAO-A) inhibitory peptides. The results demonstrated that a combination of swelling, ultrasound and alkaline dissolution was found to be the best extraction method with a protein extraction percentage of 82.29%; The alkaline protease hydrolysate (APH) possessed the best MAO-A inhibitory activity with the IC50 of 3.437 mg mL−1, and the inhibitory activity of the ultrafiltrated fraction APH-III (< 3 kDa) can reach 73.22 ± 1.31% at 6 mg mL−1. Then, 14 peptides were identified from APH-III by LC–MS/MS. Molecular docking indicated that the top high-binding peptides TEGKIPFWEGQ and GVKYGLHEVDEGATKIVQYL may interacted with MAO-A through some hydrogen bonds and hydrophobic forces. In conclusion, C. reinhardtii-derived protein could be potential source of bioactive peptides with inhibitory effects on depression-related enzyme MAO-A.