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Effect of ionic strength and temperature on interaction between fish myoglobin and myofibrillar proteins.
J Food Sci. 2007 Mar; 72(2):C89-95.JF

Abstract

The effects of ionic strength (0, 0.3, and 0.6 M KCl) and temperature (4 and 25 degrees C) on the interaction between fish myoglobin and myofibrillar proteins were investigated in a model system. Increases in the relative content of bound myoglobin and metmyoglobin formation in myoglobin-natural actomyosin (NAM) mixtures with concurrent decreases in whiteness and Ca(2+)-ATPase activity were observed with increasing ionic strength (P < 0.05). The relative content of bound myoglobin and the oxidation of oxymyoglobin were generally greater at 25 degrees C than at 4 degrees C (P < 0.05). Binding of myoglobin to NAM resulted in decreased whiteness (P < 0.05). Ca(2+)-ATPase was not affected by temperature (P > 0.05). SDS-PAGE patterns of protein samples suggested that myoglobin-NAM interactions did not involve disulfide bonds. The formation of high-molecular-weight aggregates (>206 kDa) was observed and was more pronounced at higher ionic strength and higher temperature.

Authors+Show Affiliations

Dept. of Food Technology, Faculty of Agro-Industry, Prince of Songkla Univ., Hat Yai, 90112, Thailand.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

Language

eng

PubMed ID

17995830

Citation

Chaijan, M, et al. "Effect of Ionic Strength and Temperature On Interaction Between Fish Myoglobin and Myofibrillar Proteins." Journal of Food Science, vol. 72, no. 2, 2007, pp. C89-95.
Chaijan M, Benjakul S, Visessanguan W, et al. Effect of ionic strength and temperature on interaction between fish myoglobin and myofibrillar proteins. J Food Sci. 2007;72(2):C89-95.
Chaijan, M., Benjakul, S., Visessanguan, W., Lee, S., & Faustman, C. (2007). Effect of ionic strength and temperature on interaction between fish myoglobin and myofibrillar proteins. Journal of Food Science, 72(2), C89-95.
Chaijan M, et al. Effect of Ionic Strength and Temperature On Interaction Between Fish Myoglobin and Myofibrillar Proteins. J Food Sci. 2007;72(2):C89-95. PubMed PMID: 17995830.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Effect of ionic strength and temperature on interaction between fish myoglobin and myofibrillar proteins. AU - Chaijan,M, AU - Benjakul,S, AU - Visessanguan,W, AU - Lee,S, AU - Faustman,C, PY - 2007/11/13/pubmed PY - 2007/12/15/medline PY - 2007/11/13/entrez SP - C89 EP - 95 JF - Journal of food science JO - J Food Sci VL - 72 IS - 2 N2 - The effects of ionic strength (0, 0.3, and 0.6 M KCl) and temperature (4 and 25 degrees C) on the interaction between fish myoglobin and myofibrillar proteins were investigated in a model system. Increases in the relative content of bound myoglobin and metmyoglobin formation in myoglobin-natural actomyosin (NAM) mixtures with concurrent decreases in whiteness and Ca(2+)-ATPase activity were observed with increasing ionic strength (P < 0.05). The relative content of bound myoglobin and the oxidation of oxymyoglobin were generally greater at 25 degrees C than at 4 degrees C (P < 0.05). Binding of myoglobin to NAM resulted in decreased whiteness (P < 0.05). Ca(2+)-ATPase was not affected by temperature (P > 0.05). SDS-PAGE patterns of protein samples suggested that myoglobin-NAM interactions did not involve disulfide bonds. The formation of high-molecular-weight aggregates (>206 kDa) was observed and was more pronounced at higher ionic strength and higher temperature. SN - 1750-3841 UR - https://www.unboundmedicine.com/medline/citation/17995830/Effect_of_ionic_strength_and_temperature_on_interaction_between_fish_myoglobin_and_myofibrillar_proteins_ L2 - https://doi.org/10.1111/j.1750-3841.2006.00236.x DB - PRIME DP - Unbound Medicine ER -