The Characterization of Myoglobin and Myoglobin‐Induced Lipid Oxidation in Frigate Mackerel. Issue 6 (29th February 2016)
- Record Type:
- Journal Article
- Title:
- The Characterization of Myoglobin and Myoglobin‐Induced Lipid Oxidation in Frigate Mackerel. Issue 6 (29th February 2016)
- Main Title:
- The Characterization of Myoglobin and Myoglobin‐Induced Lipid Oxidation in Frigate Mackerel
- Authors:
- Zheng, Zhenxiao
Lin, Sensen
Xue, Jing
Shen, Qing
Feng, Junli
Jin, Renyao
Dai, Zhiyuan - Abstract:
- Abstract: Myoglobin (Mb) was isolated and purified from the dark muscle of Frigate mackerel ( Auxis thazard ). After ion‐exchange chromatography, the purity of Mb reached 91.30%. The molecule weight of Mb was 16 kDa. The results of the thermal and acid–base stability suggested that oxymyoglobin and metmyoglobin denatured rapidly at 70C and kept stable under 20C. The MetMb% was decreasing and the OxyMb% was increasing in oxymyoglobin and metmyoglobin solutions with the rise of pH. Besides, Oxymyoglobin is much more stable at neutral to alkaline pH, while metmyoglobin kept its stability at acidic to neutral pH. Mb is an effective promoter of lipid oxidation, it engaged in the oxidation as participator but not catalyst. The pro‐oxidation activity of oxymyoglobin was enhanced with decrease in pH. The pro‐oxidation activities were in the order: MetMb > OxyMb > Hemin > Fe 2+, which indicated that MetMb was a greater promoter than OxyMb. Practical Applications: Frigate mackerel is an important high yield fishes in China, which is rich in myoglobin (Mb) in muscle and contains high proportion of unsaturated fatty acids. So, the discoloration and lipid oxidation of Frigate mackerel are accelerated during storage, which lowers the quality of related products. Relevant research show that discoloration correlates closely with lipid oxidation. This article is aimed at studying the stability of Mb and lipid oxidation of muscles of Frigate mackerel during refrigerated storage. In this way,Abstract: Myoglobin (Mb) was isolated and purified from the dark muscle of Frigate mackerel ( Auxis thazard ). After ion‐exchange chromatography, the purity of Mb reached 91.30%. The molecule weight of Mb was 16 kDa. The results of the thermal and acid–base stability suggested that oxymyoglobin and metmyoglobin denatured rapidly at 70C and kept stable under 20C. The MetMb% was decreasing and the OxyMb% was increasing in oxymyoglobin and metmyoglobin solutions with the rise of pH. Besides, Oxymyoglobin is much more stable at neutral to alkaline pH, while metmyoglobin kept its stability at acidic to neutral pH. Mb is an effective promoter of lipid oxidation, it engaged in the oxidation as participator but not catalyst. The pro‐oxidation activity of oxymyoglobin was enhanced with decrease in pH. The pro‐oxidation activities were in the order: MetMb > OxyMb > Hemin > Fe 2+, which indicated that MetMb was a greater promoter than OxyMb. Practical Applications: Frigate mackerel is an important high yield fishes in China, which is rich in myoglobin (Mb) in muscle and contains high proportion of unsaturated fatty acids. So, the discoloration and lipid oxidation of Frigate mackerel are accelerated during storage, which lowers the quality of related products. Relevant research show that discoloration correlates closely with lipid oxidation. This article is aimed at studying the stability of Mb and lipid oxidation of muscles of Frigate mackerel during refrigerated storage. In this way, this work will provide reference and status for the processing and preservation of Frigate mackerel. … (more)
- Is Part Of:
- Journal of food processing and preservation. Volume 40:Issue 6(2016:Dec.)
- Journal:
- Journal of food processing and preservation
- Issue:
- Volume 40:Issue 6(2016:Dec.)
- Issue Display:
- Volume 40, Issue 6 (2016)
- Year:
- 2016
- Volume:
- 40
- Issue:
- 6
- Issue Sort Value:
- 2016-0040-0006-0000
- Page Start:
- 1438
- Page End:
- 1447
- Publication Date:
- 2016-02-29
- Subjects:
- Food -- Preservation -- Periodicals
Food industry and trade -- Periodicals
664.005 - Journal URLs:
- http://firstsearch.oclc.org ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1745-4549 ↗
http://www.blackwell-synergy.com/openurl?genre=journal&eissn=1745-4549 ↗
http://onlinelibrary.wiley.com/ ↗
http://www.blackwell-synergy.com/loi/jfpp ↗ - DOI:
- 10.1111/jfpp.12729 ↗
- Languages:
- English
- ISSNs:
- 0145-8892
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 4984.548000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 554.xml