EFFECT OF PROTEIN OXIDATION ON PARTICLE SIZE OF MYOFIBRILS

Yulong Bao, Simon Allegaert, Per Ertbjerg

Research output: Chapter in Book/Report/Conference proceedingConference contributionProfessional

Abstract

In order to study the effect of protein oxidation on the structure of myofibrils, extracted myofibrils from porcine longissimus dorsi muscle were incubated with different concentrations of the oxidant NaClO (0, 5, 10, 20 and 40 mM) at 5 ºC for 16 h. Increasing concentrations of NaClO led to a greater loss of free thiols and a larger particle size (in terms of D(v, 0.1), D(v, 0.5), D(v, 0.9), D(3, 2) and D(4, 3)) of myofibrils. Light microscope imaging showed that the myofibrils oxidized in 40 mM NaClO were less broken as compared to the non-oxidized group (0 mM NaClO). The increased structural integrity of myofibrils is likely caused by oxidation-induced protein cross-links, which resulted in a larger particle size when the myofibrils were subjected to homogenization.
Original languageEnglish
Title of host publicationProceedings of 62nd International Congress of Meat Science and Technology
Number of pages4
PublisherIcoMST
Publication dateJul 2016
Publication statusPublished - Jul 2016
MoE publication typeD3 Professional conference proceedings
Event62nd international congress of meat science and technology - Bankok, Thailand
Duration: 14 Aug 201619 Aug 2016
Conference number: 62

Fields of Science

  • 416 Food Science

Cite this

Bao, Y., Allegaert, S., & Ertbjerg, P. (2016). EFFECT OF PROTEIN OXIDATION ON PARTICLE SIZE OF MYOFIBRILS. In Proceedings of 62nd International Congress of Meat Science and Technology IcoMST.