期刊
MEAT SCIENCE
卷 108, 期 -, 页码 97-105出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.meatsci.2015.05.024
关键词
Myofibrillar protein; Protein oxidation; Transglutaminase; Cross-linking
资金
- NRI/CSREES/USDA [2008-35503-18790]
- Oversea Study Fellowship from the China Scholarship Council
Porcine myofibrillar protein (MP) was oxidatively stressed in an iron-H2O2 radical-producing system then subjected to microbial transglutaminase (TGase, E:S = 1:20) at 4 degrees C. Changes in the MP secondary structure and cross-linking site on myosin (subfragments S1, S2, rod, light meromyosin, and heavy meromyosin) after TGase treatment were investigated. Circular dichroism and FTIR recorded unraveling of helixes caused by both oxidation and TGase. The loss of alpha-helix due to TGase treatment was oxidation-dependent, namely, mild oxidation (0.1-1 mM H2O2) > non-oxidation > moderate oxidation (5-20 mM H2O2). Moreover, oxidation altered the myosin cross-linking pattern: TGase-initiated S1 cross-linking (which dominated non-oxidized MP) partially shifted to the rod under 0.1-0.5 mM H2O2 and extensively to the S2 site with 20 mM H2O2. Unraveling of the helical structure and formation of disulfide bonds due to oxidation were implicated in the altered myosin cross-linking pattern during subsequent TGase reactions. (C) 2015 Elsevier Ltd. All rights reserved.
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