Isolation and Characterization of a Pueraria lobata Protein and Its Self-assembled Nanoparticles Properties
Objective: To purify and characterize a water-soluble protein from Pueraria lobata and to fabricate its nanoparticles by heating-induced assembly. Methods: Pueraria lobata protein was purified by anion exchange chromatography High Q, and its molecular weight and amino acid sequence were determined b...
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| Format: | Article |
| Language: | zho |
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The editorial department of Science and Technology of Food Industry
2023-05-01
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| Series: | Shipin gongye ke-ji |
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| Online Access: | http://www.spgykj.com/cn/article/doi/10.13386/j.issn1002-0306.2022100193 |
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| author | Dai LIN Guanzhen GAO Jianwu ZHOU Lijing KE Pingfan RAO |
| author_facet | Dai LIN Guanzhen GAO Jianwu ZHOU Lijing KE Pingfan RAO |
| author_sort | Dai LIN |
| collection | DOAJ |
| description | Objective: To purify and characterize a water-soluble protein from Pueraria lobata and to fabricate its nanoparticles by heating-induced assembly. Methods: Pueraria lobata protein was purified by anion exchange chromatography High Q, and its molecular weight and amino acid sequence were determined by SDS-PAGE and N-terminal sequencing. The particle size, optical dispersion intensity and Zeta potential of protein nanoparticles were measured by laser-scattering particle analyzer. The drug loading efficiency of the nanocarrier was determined by chromatography. Results: A major water-soluble protein, named PP, was purified from Pueraria lobata and sequenced with a N-terminal amino acid sequence of DFVYDMCGNVLNGGTYYIL. PP was identified as a novel trypsin inhibitor by NCBI database searching and rypsin inhibitory assay. PP was also well-stabilized in the pH2~10 and 20~50 °C ranges. After heating PP solution (0.1 mg/mL, pH6.0) for 60 minutes at 100 ℃, homogenous nanoparticles (PP-NPs) were harvested. These PP-NPs had a particle size of 172.78 nm and a Zeta potential of −25.40 mV. The puerarin and berberine were effectively loaded onto PP-NPs, with loading efficiency of 33.83% and 24.61%, respectively. Conclusion: The major water-soluble Pueraria lobata protein PP can be fabricated into protein nanoparticles by heating-induced assembly, indicating a potential as drug carriers. |
| first_indexed | 2024-03-12T13:33:31Z |
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| id | doaj.art-a01abe6824f74b63bf062da341c1e291 |
| institution | Directory Open Access Journal |
| issn | 1002-0306 |
| language | zho |
| last_indexed | 2024-03-12T13:33:31Z |
| publishDate | 2023-05-01 |
| publisher | The editorial department of Science and Technology of Food Industry |
| record_format | Article |
| series | Shipin gongye ke-ji |
| spelling | doaj.art-a01abe6824f74b63bf062da341c1e2912023-08-24T06:01:46ZzhoThe editorial department of Science and Technology of Food IndustryShipin gongye ke-ji1002-03062023-05-01449202610.13386/j.issn1002-0306.20221001932022100193-9Isolation and Characterization of a Pueraria lobata Protein and Its Self-assembled Nanoparticles PropertiesDai LIN0Guanzhen GAO1Jianwu ZHOU2Lijing KE3Pingfan RAO4College of Public Health, Fujian Medical University, Fuzhou 350122, ChinaCollege of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, ChinaCollege of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, ChinaCollege of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, ChinaCollege of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, ChinaObjective: To purify and characterize a water-soluble protein from Pueraria lobata and to fabricate its nanoparticles by heating-induced assembly. Methods: Pueraria lobata protein was purified by anion exchange chromatography High Q, and its molecular weight and amino acid sequence were determined by SDS-PAGE and N-terminal sequencing. The particle size, optical dispersion intensity and Zeta potential of protein nanoparticles were measured by laser-scattering particle analyzer. The drug loading efficiency of the nanocarrier was determined by chromatography. Results: A major water-soluble protein, named PP, was purified from Pueraria lobata and sequenced with a N-terminal amino acid sequence of DFVYDMCGNVLNGGTYYIL. PP was identified as a novel trypsin inhibitor by NCBI database searching and rypsin inhibitory assay. PP was also well-stabilized in the pH2~10 and 20~50 °C ranges. After heating PP solution (0.1 mg/mL, pH6.0) for 60 minutes at 100 ℃, homogenous nanoparticles (PP-NPs) were harvested. These PP-NPs had a particle size of 172.78 nm and a Zeta potential of −25.40 mV. The puerarin and berberine were effectively loaded onto PP-NPs, with loading efficiency of 33.83% and 24.61%, respectively. Conclusion: The major water-soluble Pueraria lobata protein PP can be fabricated into protein nanoparticles by heating-induced assembly, indicating a potential as drug carriers.http://www.spgykj.com/cn/article/doi/10.13386/j.issn1002-0306.2022100193pueraria lobatananoparticlesself-assemblytrypsin inhibitor |
| spellingShingle | Dai LIN Guanzhen GAO Jianwu ZHOU Lijing KE Pingfan RAO Isolation and Characterization of a Pueraria lobata Protein and Its Self-assembled Nanoparticles Properties Shipin gongye ke-ji pueraria lobata nanoparticles self-assembly trypsin inhibitor |
| title | Isolation and Characterization of a Pueraria lobata Protein and Its Self-assembled Nanoparticles Properties |
| title_full | Isolation and Characterization of a Pueraria lobata Protein and Its Self-assembled Nanoparticles Properties |
| title_fullStr | Isolation and Characterization of a Pueraria lobata Protein and Its Self-assembled Nanoparticles Properties |
| title_full_unstemmed | Isolation and Characterization of a Pueraria lobata Protein and Its Self-assembled Nanoparticles Properties |
| title_short | Isolation and Characterization of a Pueraria lobata Protein and Its Self-assembled Nanoparticles Properties |
| title_sort | isolation and characterization of a pueraria lobata protein and its self assembled nanoparticles properties |
| topic | pueraria lobata nanoparticles self-assembly trypsin inhibitor |
| url | http://www.spgykj.com/cn/article/doi/10.13386/j.issn1002-0306.2022100193 |
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