대장균과 효모를 이용한 lunasin peptide의 생산 및 histone acetylation 억제활성
The Production of Lunasin Peptide Using E. coli and P. pastoris, and Inhibitory Effect of Histone Acetylation
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초록
본 연구는 항암 단백질로 알려진 lunasin peptide의 산업적활용성을 높이고자 lunasin peptide를 생산할 수 있는 시스템을개발하고, 생산된 lunasin peptide가 식물유래 lunasin peptide 의 생리활성을 가지는지 chromatin binding 활성과 histone acetylation 억제활성을 통해 평가하였다. 그 결과 E. coli와 P. pastoris를 활용하여 재조합 lunasin peptide를 생산했으며, 생산 된 재조합 lunasin 펩타이드가 식물유래 lunasin peptide의chromatin binding 활성과 histone acetylation 억제활성을 나타냄을 확인할 수 있었다. 따라서, 본 실험 연구의결과를 토대로 lunasin 펩타이드의 대량생산이 진행된다면 천연물 유래 생리활성 물질로서 효과적이면서도 안전한 기능성 식품소재로의산업적 활용이 가능할 것으로 기대된다.
Abstract
In this study, we produced the recombinant lunasin peptide using E. coli and P. pastoris, and evaluated biological activity of the recombinant lunasin peptide. Lunasin peptide was produced from E. coli transfected with pPGEX-lunasin expression vector and P. pastoris GS115 transfected with pPIC-lunasin expression vector. These recombinant lunasin peptides were similar to the synthetic lunasin peptide in the identification by LC-ESI-MS. In addition, the recombinant lunasin peptide from E. coli and P. pastoris was bound in the chromatin, and inhibited histone acetylation and the activity of histone acetyltransferase. These findings suggest that the production of the lunasin peptide using E. coli and P. pastoris will be useful for industrial utilization of lunasin peptide.
참고문헌 (13)
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