Oxidative mechanism of chicken wooden breast myofibrillar protein
To explore the oxidation mechanism of wooden breast myofibrillar protein (WBMP), oxidative breast MP (OBMP) was obtained from different doses (3, 10, and 20 mmol/L) of H2O2 oxidized normal breast MP (NBMP). The results showed that the Zeta-potential, particle size, solubility, sulfhydryl, and carbon...
Saved in:
| Main Authors: | , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Tsinghua University Press
2024-11-01
|
| Series: | Food Science and Human Wellness |
| Subjects: | |
| Online Access: | https://www.sciopen.com/article/10.26599/FSHW.2023.9250026 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1841550085600575488 |
|---|---|
| author | Ke Wang Yimin Zhang Jingxin Sun |
| author_facet | Ke Wang Yimin Zhang Jingxin Sun |
| author_sort | Ke Wang |
| collection | DOAJ |
| description | To explore the oxidation mechanism of wooden breast myofibrillar protein (WBMP), oxidative breast MP (OBMP) was obtained from different doses (3, 10, and 20 mmol/L) of H2O2 oxidized normal breast MP (NBMP). The results showed that the Zeta-potential, particle size, solubility, sulfhydryl, and carbonyl contents of OBMP-3 (3 mmol/L, low-dose free radicals) and WBMP were similar. Fluorescence spectrum analysis showed that the oxidation of low-dose free radicals led to a significant increase in the surface hydrophobicity (from 214.03 ± 10.03 to 393.50 ± 10.33) and tryptophan fluorescence intensity (from 185.71 to 568.32). In addition, the α-helix content of WBMP decreased significantly from (37.46 ± 1.15)% (NBMP) to (34.70 ± 2.04)%, while β-sheet and random coil contents increased significantly (P < 0.05) from (14.37 ± 0.69)% and (22.24 ± 0.78)% (NBMP) to (17.70 ± 0.87)% and (25.20 ± 1.47)% (WBMP). In summary, low-dose free radical oxidation attacks protein groups, inducing secondary and tertiary structural changes, leading to the formation of WBMP. This work will provide a theoretical basis at the molecular level for exploring the mechanism of functional degradation of WBMP. |
| format | Article |
| id | doaj-art-1cfd4ee690854549813131f319096253 |
| institution | Kabale University |
| issn | 2097-0765 2213-4530 |
| language | English |
| publishDate | 2024-11-01 |
| publisher | Tsinghua University Press |
| record_format | Article |
| series | Food Science and Human Wellness |
| spelling | doaj-art-1cfd4ee690854549813131f3190962532025-01-10T06:57:02ZengTsinghua University PressFood Science and Human Wellness2097-07652213-45302024-11-011363415342310.26599/FSHW.2023.9250026Oxidative mechanism of chicken wooden breast myofibrillar proteinKe Wang0Yimin Zhang1Jingxin Sun2College of Food Science & Engineering, Qingdao Agricultural University, Qingdao 266109, ChinaCollege of Food Science & Engineering, Shandong Agricultural University, Tai’an 271018, ChinaCollege of Food Science & Engineering, Qingdao Agricultural University, Qingdao 266109, ChinaTo explore the oxidation mechanism of wooden breast myofibrillar protein (WBMP), oxidative breast MP (OBMP) was obtained from different doses (3, 10, and 20 mmol/L) of H2O2 oxidized normal breast MP (NBMP). The results showed that the Zeta-potential, particle size, solubility, sulfhydryl, and carbonyl contents of OBMP-3 (3 mmol/L, low-dose free radicals) and WBMP were similar. Fluorescence spectrum analysis showed that the oxidation of low-dose free radicals led to a significant increase in the surface hydrophobicity (from 214.03 ± 10.03 to 393.50 ± 10.33) and tryptophan fluorescence intensity (from 185.71 to 568.32). In addition, the α-helix content of WBMP decreased significantly from (37.46 ± 1.15)% (NBMP) to (34.70 ± 2.04)%, while β-sheet and random coil contents increased significantly (P < 0.05) from (14.37 ± 0.69)% and (22.24 ± 0.78)% (NBMP) to (17.70 ± 0.87)% and (25.20 ± 1.47)% (WBMP). In summary, low-dose free radical oxidation attacks protein groups, inducing secondary and tertiary structural changes, leading to the formation of WBMP. This work will provide a theoretical basis at the molecular level for exploring the mechanism of functional degradation of WBMP.https://www.sciopen.com/article/10.26599/FSHW.2023.9250026wooden breastmyofibrillar proteinfree radicaloxidationphysicochemical propertymolecular structure |
| spellingShingle | Ke Wang Yimin Zhang Jingxin Sun Oxidative mechanism of chicken wooden breast myofibrillar protein Food Science and Human Wellness wooden breast myofibrillar protein free radical oxidation physicochemical property molecular structure |
| title | Oxidative mechanism of chicken wooden breast myofibrillar protein |
| title_full | Oxidative mechanism of chicken wooden breast myofibrillar protein |
| title_fullStr | Oxidative mechanism of chicken wooden breast myofibrillar protein |
| title_full_unstemmed | Oxidative mechanism of chicken wooden breast myofibrillar protein |
| title_short | Oxidative mechanism of chicken wooden breast myofibrillar protein |
| title_sort | oxidative mechanism of chicken wooden breast myofibrillar protein |
| topic | wooden breast myofibrillar protein free radical oxidation physicochemical property molecular structure |
| url | https://www.sciopen.com/article/10.26599/FSHW.2023.9250026 |
| work_keys_str_mv | AT kewang oxidativemechanismofchickenwoodenbreastmyofibrillarprotein AT yiminzhang oxidativemechanismofchickenwoodenbreastmyofibrillarprotein AT jingxinsun oxidativemechanismofchickenwoodenbreastmyofibrillarprotein |