The effect of Cytochalasin B and Jasplakinolide on depolymerization of actin filaments in goose muscles during postmortem conditioning

Changyu Zhou; Ying Wang; Daodong Pan; Yangying Sun; Jinxuan Cao

doi:10.1016/j.foodres.2016.10.032

The effect of Cytochalasin B and Jasplakinolide on depolymerization of actin filaments in goose muscles during postmortem conditioning

Food Res Int. 2016 Dec:90:1-7. doi: 10.1016/j.foodres.2016.10.032. Epub 2016 Oct 29.

Authors

Changyu Zhou¹, Ying Wang¹, Daodong Pan¹, Yangying Sun¹, Jinxuan Cao²

Affiliations

¹ Key Laboratory of Animal Protein Food Processing Technology of Zhejiang Province, Ningbo University, Ningbo 315211, China.
² Key Laboratory of Animal Protein Food Processing Technology of Zhejiang Province, Ningbo University, Ningbo 315211, China. Electronic address: caojinxuan@nbu.edu.cn.

PMID: 29195861
DOI: 10.1016/j.foodres.2016.10.032

Abstract

Breast muscles of twenty-four Eastern Zhejiang White Geese were randomly divided into three groups: control, Cytochalasin B (Cyt B) and Jasplakinolide (Jasp) treatments during postmortem conditioning. The myofibrillar fraction index (MFI), actin filaments and the levels of F-actin, G-actin and actin associated proteins (cofilins and tropomodulins) during conditioning were investigated. In control, the degraded tropomodulins, increased G-actin and disrupted actin filaments were observed at 4 and 7days; the increase of MFI and decrease of F-actin content were shown during conditioning. Cyt B treatments accelerated the transformation from F-actin to G-actin, weakened actin filaments and increased MFI compared to the control, while Jasp gained the opposite effect against Cyt B. We concluded that depolymerization of actin filaments regulated by tropomodulins contributed to myofibrillar fraction during conditioning. This work provided a new pathway of tenderization by the depolymerization of actin filaments.

Keywords: Cytochalasin B; Depolymerizing; G-actin; Jasplakinolide; Myofibrillar fraction index; Tenderization.