We report the chloroplast (cp) genome sequence of tartary buckwheat (Fagopyrum tataricum) obtained by next-generation sequencing technology and compared this with the previously reported common buckwheat (F. esculentum ssp. ancestrale) cp genome. The cp genome of F. tataricum has a total sequence length of 159,272 bp, which is 327 bp shorter than the common buckwheat cp genome. The cp gene content, order, and orientation are similar to those of common buckwheat, but with some structural variation at tandem and palindromic repeat frequencies and junction areas. A total of seven InDels (around 100 bp) were found within the intergenic sequences and the ycf1 gene. Copy number variation of the 21-bp tandem repeat varied in F. tataricum (four repeats) and F. esculentum (one repeat), and the InDel of the ycf1 gene was 63 bp long. Nucleotide and amino acid have highly conserved coding sequence with about 98% homology and four genes—rpoC2, ycf3, accD, and clpP—have high synonymous (Ks) value. PCR based InDel markers were applied to diverse genetic resources of F. tataricum and F. esculentum, and the amplicon size was identical to that expected in silico. Therefore, these InDel markers are informative biomarkers to practically distinguish raw or processed buckwheat products derived from F. tataricum and F. esculentum.

No abstract

This study was designed to investigate the effect of cooking on in vitro digestibility and peptide profiling of pork protein. We simulated gastrointestinal digestion of cooked pork that was treated with pepsin alone or followed by trypsin treatment. Digested products were identified using matrix-assisted laser desorption/ionization–time-of-flight mass spectrometry and liquid chromatography–mass spectrometry analyses. Cooking led to a reduction (p < 0.05) in digestibility and band intensities on sodium dodecyl sulfate–polyacrylamide gel electrophoresis gels. Peptide profiling and identification analyses also showed significant difference (p < 0.05) in the m/z ranges and number of peptides from the pepsin-digested products between raw (4 °C) and very well done samples (100 °C). Peptides sequenced from pepsin-digested samples under lower degrees of doneness disappeared as the temperature increased. Meanwhile, the trypsin cleavages appeared more consistent among different degrees of cooking. Further work may be needed to evaluate the bioavailability of the digested products under different cooking temperatures.

No abstract

No abstract