Effects of l-arginine and l-histidine on heat-induced aggregation of fish myosin: Bighead carp (Aristichthys nobilis). (15th October 2019)
- Record Type:
- Journal Article
- Title:
- Effects of l-arginine and l-histidine on heat-induced aggregation of fish myosin: Bighead carp (Aristichthys nobilis). (15th October 2019)
- Main Title:
- Effects of l-arginine and l-histidine on heat-induced aggregation of fish myosin: Bighead carp (Aristichthys nobilis)
- Authors:
- Gao, Ruichang
Shi, Tong
Sun, Quancai
Li, Xiuting
McClements, David Julian
Yuan, Li - Abstract:
- Highlights: Turbidity and particle diameter of myosin decreased with Arg/His. The hydrophobicity of myosin containing Arg/His increased after two-step heating. Positively charged Arg theoretically was bound to negatively charged myosin. R-group of Arg/His might interact with unfolding aromatic residue of myosin. Arg showed a higher ability on suppressing myosin aggregation than that of His. Abstract: This research focused on the effects ofl -arginine (l -Arg) andl -histidine (l -His) on the heat-induced aggregation of fish myosin.l -Arg/l -His increased the pH of the myosin solution from 6.82 to 8.74 and 7.24, respectively, and decreased the turbidity, aggregate size, shear modulus, and breaking force. The incorporation ofl -Arg/l -His decreased the surface hydrophobicity during setting, but increased it during the two-step heating. The heat-induced aggregation of myosin was suppressed by both amino acids, with the inhibitory effect being greater forl -Arg thanl -His. On one hand, the change in the pH played a critical role in suppressing the heat-induced aggregation of myosin. On the other hand, the characteristics ofl -Arg/l -His themselves, such as net charges and particular R-groups, were another main contributor to aggregation suppression. Particularly, l -Arg/l -His could interact with exposed aromatic residues of myosin, and the interactions may dominate and overwhelm the burial of aromatic residues during two-step heating.
- Is Part Of:
- Food chemistry. Volume 295(2019)
- Journal:
- Food chemistry
- Issue:
- Volume 295(2019)
- Issue Display:
- Volume 295, Issue 2019 (2019)
- Year:
- 2019
- Volume:
- 295
- Issue:
- 2019
- Issue Sort Value:
- 2019-0295-2019-0000
- Page Start:
- 320
- Page End:
- 326
- Publication Date:
- 2019-10-15
- Subjects:
- l-Arginine -- l-Histidine -- Myosin -- Heat-induced aggregation -- Suppression -- pH -- Surface hydrophobicity
Food -- Analysis -- Periodicals
Food -- Composition -- Periodicals
664 - Journal URLs:
- http://www.sciencedirect.com/science/journal/03088146 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.foodchem.2019.05.095 ↗
- Languages:
- English
- ISSNs:
- 0308-8146
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.284000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 10969.xml