Effect of ice structuring protein on the microstructure and myofibrillar protein structure of mirror carp (Cyprinus carpio L.) induced by freeze-thaw processes. (March 2021)
- Record Type:
- Journal Article
- Title:
- Effect of ice structuring protein on the microstructure and myofibrillar protein structure of mirror carp (Cyprinus carpio L.) induced by freeze-thaw processes. (March 2021)
- Main Title:
- Effect of ice structuring protein on the microstructure and myofibrillar protein structure of mirror carp (Cyprinus carpio L.) induced by freeze-thaw processes
- Authors:
- Du, Xin
Li, Haijing
Dong, Chunhui
Ren, Yanming
Pan, Nan
Kong, Baohua
Liu, Hongyu
Xia, Xiufang - Abstract:
- Abstract: The cryoprotective effect of ice structuring protein (ISP) on the microstructure and myofibrillar protein (MP) structure of mirror carp induced by freeze-thaw (F-T) processes was surveyed. The average diameter of ice crystals of those without ISP increased (from 130 to 220 μm), and the carbonyl content and 2θ value were also increased, meanwhile, the sulfhydryl, free amine, α-helix content, fluorescence intensity (FI) and peak intensity were significantly decreased after five F-T processes ( P < 0.05). When the addition of ISP, the size of ice crystal and the change in MP structure of ISP-treated sample was smaller than those without ISP in a single F-T period. The average diameter of ice crystals of ISP-treated sample was 17.5% lower than those without ISP after three F-T processes. The carbonyl content of ISP-treated sample was 16.5% lower than those without ISP after five F-T processes. The α-helix and FI of ISP-treated sample were 58.2% and 816 A.U., higher than those without ISP. The physical stability of the MP was increased after ISP treated. Hence, ISP could protect muscle fibers by inhibiting the extension of ice crystals, and improve the stability of the MP structure. Highlights: Freeze-thaw damaged the muscle tissue and protein structure of mirror carp. Ice structuring protein minimized the freeze-thaw damage to fish microstructure. Ice structuring protein curbed freeze-thaw induced changes in myofibrillar protein structure. Ice structuring proteinAbstract: The cryoprotective effect of ice structuring protein (ISP) on the microstructure and myofibrillar protein (MP) structure of mirror carp induced by freeze-thaw (F-T) processes was surveyed. The average diameter of ice crystals of those without ISP increased (from 130 to 220 μm), and the carbonyl content and 2θ value were also increased, meanwhile, the sulfhydryl, free amine, α-helix content, fluorescence intensity (FI) and peak intensity were significantly decreased after five F-T processes ( P < 0.05). When the addition of ISP, the size of ice crystal and the change in MP structure of ISP-treated sample was smaller than those without ISP in a single F-T period. The average diameter of ice crystals of ISP-treated sample was 17.5% lower than those without ISP after three F-T processes. The carbonyl content of ISP-treated sample was 16.5% lower than those without ISP after five F-T processes. The α-helix and FI of ISP-treated sample were 58.2% and 816 A.U., higher than those without ISP. The physical stability of the MP was increased after ISP treated. Hence, ISP could protect muscle fibers by inhibiting the extension of ice crystals, and improve the stability of the MP structure. Highlights: Freeze-thaw damaged the muscle tissue and protein structure of mirror carp. Ice structuring protein minimized the freeze-thaw damage to fish microstructure. Ice structuring protein curbed freeze-thaw induced changes in myofibrillar protein structure. Ice structuring protein enhanced the physical structure stability of myofibrillar protein. … (more)
- Is Part Of:
- Lebensmittel-Wissenschaft + Technologie =. Volume 139(2021)
- Journal:
- Lebensmittel-Wissenschaft + Technologie =
- Issue:
- Volume 139(2021)
- Issue Display:
- Volume 139, Issue 2021 (2021)
- Year:
- 2021
- Volume:
- 139
- Issue:
- 2021
- Issue Sort Value:
- 2021-0139-2021-0000
- Page Start:
- Page End:
- Publication Date:
- 2021-03
- Subjects:
- Cyprinus carpio L. -- Ice structuring protein -- Myofibrillar protein -- Ice crystals -- Freeze-thaw treatment
Food industry and trade -- Periodicals
Food -- Composition -- Periodicals
Microbiology -- Periodicals
Nutrition -- Periodicals
664.005 - Journal URLs:
- http://www.sciencedirect.com/science/journal/00236438 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.lwt.2020.110570 ↗
- Languages:
- English
- ISSNs:
- 0023-6438
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3983.070000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 19602.xml