Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 50, Issue 17, Pages 4803-4811Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jf0116000
Keywords
CD; DSC; light meromyosin; myosin; recombinant protein; thermodynamic properties; walleye pollack
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The thermodynamic properties of myosin and its C-terminal fragment, light meromyosin (LMM), from walleye pollack, a typical cold-water fish efficiently utilized on an industrial scale, were analyzed by using differential scanning calorimetry (DSC) and circular dichroism (CD) spectrometry. Recombinant walleye pollack LMM expressed in Escherichia coli was also subjected to DSC and CID measurements for reference. The two proteins prepared from frozen surimi showed three endothermic peaks, the transition temperatures (T-m) of which were quite similar, although overall DSC patterns differed considerably from one another. Their a-helical contents determined by CD were low compared to values reported before for other species. On the other hand, recombinant LMM gave four endothermic peaks at 27.4, 30.8, 36.5, and 43.4 degreesC in DSC and showed an a-helical content of similar to80%. The peak at 27.4 degreesC could not be observed in walleye pollack LMM prepared from frozen surimi and thus was possibly attributed to its C terminus, because this extreme C-terminal region is supposedly truncated during preparation of LMM by tryptic digestion.
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