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| Isolation and stability of antimicrobial peptide fraction from Prinsepia utilis Royle |
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| DOI： |
| KeyWord:Prinsepia utilis Royle antimicrobial peptides separation antibacterial activity stability |
| FundProject:国家自然科学基金地区项目（31960462）；云南省基础研究计划面上项目（2019FB052）；云南省农业联合专项重点项目（202101BD070001-013）；云南省青年科技人才托举工程项目 |
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| Abstract: |
| In order to make high value use of the proteins in the by-products of Prinsepia utilis Royle oil extraction, Prinsepia utilis Royle proteins were extracted from the meal of Prinsepia utilis Royle and then hydrolyzed to prepare hydrolysates. The antimicrobial peptide fractions were screened from the hydrolysates by using live bacterial adsorption combined with reversed-phase high-performance liquid chromatography (RP-HPLC), their antibacterial activities were evaluated, and the stability of the fraction with the best antibacterial activity was analyzed. The results showed that among the three antimicrobial peptide fractions (F1, F2 and F3) screened, the F2 fraction had the best antibacterial activity, and its antibacterial activities against Staphylococcus aureus and Escherichia coli reached 45.5% and 39.1%, respectively, at a mass concentration of 10 mg/mL. The antibacterial activity of the antimicrobial peptide fraction F2 was reduced with the increase of temperature and salt solution concentration, and its optimal pH was 6.0, and it was extremely unstable in an acidic environment. The antimicrobial peptide fraction F2 was poorly tolerated by acid protease, alkaline protease, pepsin and trypsin, and better tolerated by neutral protease. In conclusion, the enzymatic hydrolysates of protein in the meal of Prinsepia utilis Royle have antibacterial activity, and has potential for the development of antimicrobial peptides from Prinsepia utilis Royle. |
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