Technology optimization on preparing angiotensin I-converting enzyme inhibitory peptides with enzymatic hydrolysis of major royal jelly proteins by utilizing pepsin and trypsin
Major royal jelly proteins (MRJPs) were hydrolyzed with pepsin and trypsin, and the effects of substrate concentration, pH value, enzyme response time and proteinase concentration on the hydrolysis efficiency were analyzed, and the orthogonal test analysis of combined action of pepsin and trypsin we...
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| Format: | Article |
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Zhejiang University Press
2012-07-01
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| Series: | 浙江大学学报. 农业与生命科学版 |
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| Online Access: | https://www.academax.com/doi/10.3785/j.issn.1008-9209.2012.04.021 |
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| author | ZHANG Wei-guang YUAN Peng YIN Zhi-hong QIU Wei SHEN Li-rong |
| author_facet | ZHANG Wei-guang YUAN Peng YIN Zhi-hong QIU Wei SHEN Li-rong |
| author_sort | ZHANG Wei-guang |
| collection | DOAJ |
| description | Major royal jelly proteins (MRJPs) were hydrolyzed with pepsin and trypsin, and the effects of substrate concentration, pH value, enzyme response time and proteinase concentration on the hydrolysis efficiency were analyzed, and the orthogonal test analysis of combined action of pepsin and trypsin were done. The enzymolysis products of MRJPs (H-MRJPs) were separated to prepare the angiotensin I-converting enzyme (ACE) inhibitory peptides by ultrafiltration technique. The results showed that the optimized technical parameters were as follows: enzymatic hydrolysis of MRJPs with 1% pepsin at pH 2.0 for 2 h, then 1% trypsin at pH 7.5 for 2 h at 37 ℃. The degree of hydrolysis and total nitrogen recovery of MRJPs under the optimal condition were 28.7% and 35.5%, respectively. No obvious protein bands were shown for enzymolysis products of MRJPs (H-MRJPs) by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Three kinds of ACE inhibitory peptides, ranging from <1, 1-5 and >5 ku, were separated by ultrafiltration separation of H-MRJPs. The 50% inhibitory concentration (IC50) values of the three kinds of ACE inhibitory peptides were 0.33, 0.61, and 1.09 mg·mL<sup>-1</sup>, respectively, which exhibited that the peptides with molecular mass <1 ku possessed most high ACE inhibitory activity. The results above provide a scientific basis for developing functional food of antihypertension. |
| format | Article |
| id | doaj-art-34af76172d51478f841cd7c4ea2aff17 |
| institution | Kabale University |
| issn | 1008-9209 2097-5155 |
| language | English |
| publishDate | 2012-07-01 |
| publisher | Zhejiang University Press |
| record_format | Article |
| series | 浙江大学学报. 农业与生命科学版 |
| spelling | doaj-art-34af76172d51478f841cd7c4ea2aff172025-08-20T03:34:18ZengZhejiang University Press浙江大学学报. 农业与生命科学版1008-92092097-51552012-07-013851151810.3785/j.issn.1008-9209.2012.04.02110089209Technology optimization on preparing angiotensin I-converting enzyme inhibitory peptides with enzymatic hydrolysis of major royal jelly proteins by utilizing pepsin and trypsinZHANG Wei-guangYUAN PengYIN Zhi-hongQIU WeiSHEN Li-rongMajor royal jelly proteins (MRJPs) were hydrolyzed with pepsin and trypsin, and the effects of substrate concentration, pH value, enzyme response time and proteinase concentration on the hydrolysis efficiency were analyzed, and the orthogonal test analysis of combined action of pepsin and trypsin were done. The enzymolysis products of MRJPs (H-MRJPs) were separated to prepare the angiotensin I-converting enzyme (ACE) inhibitory peptides by ultrafiltration technique. The results showed that the optimized technical parameters were as follows: enzymatic hydrolysis of MRJPs with 1% pepsin at pH 2.0 for 2 h, then 1% trypsin at pH 7.5 for 2 h at 37 ℃. The degree of hydrolysis and total nitrogen recovery of MRJPs under the optimal condition were 28.7% and 35.5%, respectively. No obvious protein bands were shown for enzymolysis products of MRJPs (H-MRJPs) by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Three kinds of ACE inhibitory peptides, ranging from <1, 1-5 and >5 ku, were separated by ultrafiltration separation of H-MRJPs. The 50% inhibitory concentration (IC50) values of the three kinds of ACE inhibitory peptides were 0.33, 0.61, and 1.09 mg·mL<sup>-1</sup>, respectively, which exhibited that the peptides with molecular mass <1 ku possessed most high ACE inhibitory activity. The results above provide a scientific basis for developing functional food of antihypertension.https://www.academax.com/doi/10.3785/j.issn.1008-9209.2012.04.021major royal jelly proteins (MRJPs)pepsin and trypsinenzymatic hydrolysis technologyultrafiltrationangiotensin I-converting enzyme inhibitory peptides |
| spellingShingle | ZHANG Wei-guang YUAN Peng YIN Zhi-hong QIU Wei SHEN Li-rong Technology optimization on preparing angiotensin I-converting enzyme inhibitory peptides with enzymatic hydrolysis of major royal jelly proteins by utilizing pepsin and trypsin 浙江大学学报. 农业与生命科学版 major royal jelly proteins (MRJPs) pepsin and trypsin enzymatic hydrolysis technology ultrafiltration angiotensin I-converting enzyme inhibitory peptides |
| title | Technology optimization on preparing angiotensin I-converting enzyme inhibitory peptides with enzymatic hydrolysis of major royal jelly proteins by utilizing pepsin and trypsin |
| title_full | Technology optimization on preparing angiotensin I-converting enzyme inhibitory peptides with enzymatic hydrolysis of major royal jelly proteins by utilizing pepsin and trypsin |
| title_fullStr | Technology optimization on preparing angiotensin I-converting enzyme inhibitory peptides with enzymatic hydrolysis of major royal jelly proteins by utilizing pepsin and trypsin |
| title_full_unstemmed | Technology optimization on preparing angiotensin I-converting enzyme inhibitory peptides with enzymatic hydrolysis of major royal jelly proteins by utilizing pepsin and trypsin |
| title_short | Technology optimization on preparing angiotensin I-converting enzyme inhibitory peptides with enzymatic hydrolysis of major royal jelly proteins by utilizing pepsin and trypsin |
| title_sort | technology optimization on preparing angiotensin i converting enzyme inhibitory peptides with enzymatic hydrolysis of major royal jelly proteins by utilizing pepsin and trypsin |
| topic | major royal jelly proteins (MRJPs) pepsin and trypsin enzymatic hydrolysis technology ultrafiltration angiotensin I-converting enzyme inhibitory peptides |
| url | https://www.academax.com/doi/10.3785/j.issn.1008-9209.2012.04.021 |
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