Structural and antioxidative properties of royal jelly protein by partial enzymatic hydrolysis
The objective of this study was to investigate the structural and antioxidative properties of royal jelly protein (RJP) at different degrees of hydrolysis (DH) by partial enzymatic hydrolysis. RJP was hydrolyzed by alcalase for 0 min, 15 min, 1 h, 5 h and 8 h to obtain hydrolysates at DH of 5.34 %,...
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| Format: | Article |
| Language: | English |
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Tsinghua University Press
2023-09-01
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| Series: | Food Science and Human Wellness |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2213453023000460 |
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| author | Shanshan Li Lingchen Tao Shiqin Peng Xinyu Yu Xiaobin Ma Fuliang Hu |
| author_facet | Shanshan Li Lingchen Tao Shiqin Peng Xinyu Yu Xiaobin Ma Fuliang Hu |
| author_sort | Shanshan Li |
| collection | DOAJ |
| description | The objective of this study was to investigate the structural and antioxidative properties of royal jelly protein (RJP) at different degrees of hydrolysis (DH) by partial enzymatic hydrolysis. RJP was hydrolyzed by alcalase for 0 min, 15 min, 1 h, 5 h and 8 h to obtain hydrolysates at DH of 5.34 %, 11.65 %, 15.19 %, 21.38 % and 23.91 %, respectively. With the increased DH, the RJP hydrolysates showed elevated antioxidative activities. The molecular weight of RJP hydrolysates was significantly decreased but their primary backbone kept unchanged. Analysis of circular dichroism spectra revealed that the enzymolysis reduced the content of α-helix but increased the contents of β-sheet, β-turn and random coil. Meanwhile, the surface hydrophobicity and fluorescence intensity of RJP hydrolysates were decreased and a red shift occurred. As the enzymolysis continued, the surface morphology of RJP was gradually changed from a sheet-like structure into microparticles. Changes in antioxidative activities and structures generally followed a DH-dependent manner, however these changes became insignificant for samples at DH beyond 20 %. Taking into consideration of both effectiveness and productivity, the optimum enzymatic duration was determined at 5 h. |
| format | Article |
| id | doaj-art-f6d56b7d7303442bb76fd4e01cb3a842 |
| institution | Kabale University |
| issn | 2213-4530 |
| language | English |
| publishDate | 2023-09-01 |
| publisher | Tsinghua University Press |
| record_format | Article |
| series | Food Science and Human Wellness |
| spelling | doaj-art-f6d56b7d7303442bb76fd4e01cb3a8422025-02-03T05:40:26ZengTsinghua University PressFood Science and Human Wellness2213-45302023-09-0112518201827Structural and antioxidative properties of royal jelly protein by partial enzymatic hydrolysisShanshan Li0Lingchen Tao1Shiqin Peng2Xinyu Yu3Xiaobin Ma4Fuliang Hu5Key laboratory of silkworm and bee resource utilization and innovation of Zhejiang Province, College of Animal Sciences, Zhejiang University, Hangzhou 310058, ChinaKey laboratory of silkworm and bee resource utilization and innovation of Zhejiang Province, College of Animal Sciences, Zhejiang University, Hangzhou 310058, ChinaKey laboratory of silkworm and bee resource utilization and innovation of Zhejiang Province, College of Animal Sciences, Zhejiang University, Hangzhou 310058, ChinaKey laboratory of silkworm and bee resource utilization and innovation of Zhejiang Province, College of Animal Sciences, Zhejiang University, Hangzhou 310058, ChinaTeagasc Food Research Centre, Moorepark, Fermoy, Co. Cork P61 C996, Ireland; Corresponding authors.Key laboratory of silkworm and bee resource utilization and innovation of Zhejiang Province, College of Animal Sciences, Zhejiang University, Hangzhou 310058, China; Corresponding authors.The objective of this study was to investigate the structural and antioxidative properties of royal jelly protein (RJP) at different degrees of hydrolysis (DH) by partial enzymatic hydrolysis. RJP was hydrolyzed by alcalase for 0 min, 15 min, 1 h, 5 h and 8 h to obtain hydrolysates at DH of 5.34 %, 11.65 %, 15.19 %, 21.38 % and 23.91 %, respectively. With the increased DH, the RJP hydrolysates showed elevated antioxidative activities. The molecular weight of RJP hydrolysates was significantly decreased but their primary backbone kept unchanged. Analysis of circular dichroism spectra revealed that the enzymolysis reduced the content of α-helix but increased the contents of β-sheet, β-turn and random coil. Meanwhile, the surface hydrophobicity and fluorescence intensity of RJP hydrolysates were decreased and a red shift occurred. As the enzymolysis continued, the surface morphology of RJP was gradually changed from a sheet-like structure into microparticles. Changes in antioxidative activities and structures generally followed a DH-dependent manner, however these changes became insignificant for samples at DH beyond 20 %. Taking into consideration of both effectiveness and productivity, the optimum enzymatic duration was determined at 5 h.http://www.sciencedirect.com/science/article/pii/S2213453023000460Royal jelly proteinAcalaseEnzymatic hydrolysisAntioxidative activityStructure |
| spellingShingle | Shanshan Li Lingchen Tao Shiqin Peng Xinyu Yu Xiaobin Ma Fuliang Hu Structural and antioxidative properties of royal jelly protein by partial enzymatic hydrolysis Food Science and Human Wellness Royal jelly protein Acalase Enzymatic hydrolysis Antioxidative activity Structure |
| title | Structural and antioxidative properties of royal jelly protein by partial enzymatic hydrolysis |
| title_full | Structural and antioxidative properties of royal jelly protein by partial enzymatic hydrolysis |
| title_fullStr | Structural and antioxidative properties of royal jelly protein by partial enzymatic hydrolysis |
| title_full_unstemmed | Structural and antioxidative properties of royal jelly protein by partial enzymatic hydrolysis |
| title_short | Structural and antioxidative properties of royal jelly protein by partial enzymatic hydrolysis |
| title_sort | structural and antioxidative properties of royal jelly protein by partial enzymatic hydrolysis |
| topic | Royal jelly protein Acalase Enzymatic hydrolysis Antioxidative activity Structure |
| url | http://www.sciencedirect.com/science/article/pii/S2213453023000460 |
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