The efficient enrichment of marine peptides from the protein hydrolysate of the marine worm Urechis unicinctus by using mesoporous materials MCM-41, SBA-15 and CMK-3. Issue 21 (17th May 2021)
- Record Type:
- Journal Article
- Title:
- The efficient enrichment of marine peptides from the protein hydrolysate of the marine worm Urechis unicinctus by using mesoporous materials MCM-41, SBA-15 and CMK-3. Issue 21 (17th May 2021)
- Main Title:
- The efficient enrichment of marine peptides from the protein hydrolysate of the marine worm Urechis unicinctus by using mesoporous materials MCM-41, SBA-15 and CMK-3
- Authors:
- Li, Xinwei
Ma, Yueyun
Zuo, Yijin
Liu, Zonghao
Wang, Qiukuan
Ren, Dandan
He, Yunhai
Cong, Haihua
Wu, Long
Zhou, Hui - Abstract:
- Abstract : Silica MCM-41 and SBA-15 and carbon CMK-3 exhibited evident enrichment ability for peptides of the protein hydrolysate of the marine worm Urechis unicinctus . Abstract : Peptides found in marine life have various specific activities due to their special growth environment, and there is increasing interest in the isolation and concentration of these biofunctional compounds. In this study, the protein hydrolysate of the marine worm Urechis unicinctus was prepared by enzymolysis and enriched by using mesoporous materials of silica MCM-41 and SBA-15 and carbon CMK-3. The differences in pore structures and elemental composition of these materials lead to differences in surface area and hydrophobicity. The adsorption capacities of peptides were 459.5 mg g −1, 431.3 mg g −1, and 626.3 mg g −1 for MCM-41, SBA-15 and CMK-3, respectively. Adsorption kinetics studies showed that the pseudo-second-order model fit the adsorption process better, where both external mass transfer and intraparticle diffusion affected the adsorption, while the Langmuir model better fit the adsorption of peptides on MCM-41 and SBA-15 and the Freundlich model was more suitable for CMK-3. Aqueous acetonitrile (ACN, 50/50, v/v) yielded the most extracted peptides. MALDI-TOF mass spectrometry of the extracted peptides showed that the three mesoporous materials, especially the CMK-3, gave good enrichment results. This study demonstrates the great potential of mesoporous materials in the enrichment ofAbstract : Silica MCM-41 and SBA-15 and carbon CMK-3 exhibited evident enrichment ability for peptides of the protein hydrolysate of the marine worm Urechis unicinctus . Abstract : Peptides found in marine life have various specific activities due to their special growth environment, and there is increasing interest in the isolation and concentration of these biofunctional compounds. In this study, the protein hydrolysate of the marine worm Urechis unicinctus was prepared by enzymolysis and enriched by using mesoporous materials of silica MCM-41 and SBA-15 and carbon CMK-3. The differences in pore structures and elemental composition of these materials lead to differences in surface area and hydrophobicity. The adsorption capacities of peptides were 459.5 mg g −1, 431.3 mg g −1, and 626.3 mg g −1 for MCM-41, SBA-15 and CMK-3, respectively. Adsorption kinetics studies showed that the pseudo-second-order model fit the adsorption process better, where both external mass transfer and intraparticle diffusion affected the adsorption, while the Langmuir model better fit the adsorption of peptides on MCM-41 and SBA-15 and the Freundlich model was more suitable for CMK-3. Aqueous acetonitrile (ACN, 50/50, v/v) yielded the most extracted peptides. MALDI-TOF mass spectrometry of the extracted peptides showed that the three mesoporous materials, especially the CMK-3, gave good enrichment results. This study demonstrates the great potential of mesoporous materials in the enrichment of marine biofunctional peptides. … (more)
- Is Part Of:
- Analytical methods. Volume 13:Issue 21(2021)
- Journal:
- Analytical methods
- Issue:
- Volume 13:Issue 21(2021)
- Issue Display:
- Volume 13, Issue 21 (2021)
- Year:
- 2021
- Volume:
- 13
- Issue:
- 21
- Issue Sort Value:
- 2021-0013-0021-0000
- Page Start:
- 2405
- Page End:
- 2414
- Publication Date:
- 2021-05-17
- Subjects:
- Chemistry, Analytic -- Periodicals
Analytical biochemistry -- Periodicals
Chemical laboratories -- Standards -- Periodicals
543.1905 - Journal URLs:
- http://pubs.rsc.org/en/Journals/JournalIssues/AY ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/d1ay00616a ↗
- Languages:
- English
- ISSNs:
- 1759-9660
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 0897.103700
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 17000.xml