Genotyping and Phenotyping of Indigenous from a New Zealand Organic Winery and Commercial Sources Using Inter-Delta and MALDI-TOF MS Typing.

We used inter-delta typing (IDT) and MALDI-TOF profiling to characterize the genetic and phenotypic diversity of 45 commercially available winemaking strains and 60 isolates from an organic winemaker from Waipara, New Zealand, as a stratified approach for predicting the commercial potential of indigenous isolates. A total of 35 IDTs were identified from the commercial strains, with another 17 novel types defined among the Waipara isolates. IDT 3 was a common type among strains associated with champagne production, and the only type in commercial strains also observed in indigenous isolates.

Characterizing lysinoalanine crosslinks in food systems: Discovery of a diagnostic ion in model peptides using MALDI mass spectrometry.

Formation of lysinoalanine protein-protein crosslinks during food processing adversely impacts nutritional value. However, mapping lysinoalanine directly in food is challenging. We characterized the fragmentation pattern of lysinoalanine crosslinks in synthetic peptide models over a range of pH and time treatments using mass spectrometry.

Insight into the self-assembly and gel formation of a bioactive peptide derived from bovine casein.

Abstract: The self-assembling and gelation properties of a bioactive peptide derived from bovine casein (FFVAPFPEVFGK) were studied in the peptide's natural form (uncapped, ) and capped with protecting groups added to both termini (capped, ). Although the natural peptide () did not demonstrate self-assembly, the capped peptide () spontaneously self-assembled and formed a self-supporting gel. Variations in peptide concentration and incubation time influenced the gel's mechanical properties, suggesting the peptide's properties could be tuned and exploited for different applications.

Unlocking the bioactivity of meat proteins: Comparison of meat and meat hydrolysate via simulated gastrointestinal digestion.

Understanding the functional attributes of meat proteins is crucial for determining their nutritional benefits. Depending on the form in which meat proteins are available, the digestive process can release peptides which are valuable for nutrition and may also possess bioactive properties, affecting physiology. Liquid chromatography - mass spectrometry (LC-MS) was used to quantitatively compare the molecular peptide features (representing non-redundant peptides), during the different stages of a simulated gastrointestinal digestion process of a minimally processed powdered meat and its enzymatically produced hydrolysate.

The protein dynamics of bovine and caprine β-lactoglobulin differ as a function of pH.

The properties of milk proteins differ between mammalian species. β-Lactoglobulin (βlg) proteins from caprine and bovine milk are sequentially and structurally highly similar, yet their physicochemical properties differ, particularly in response to pH. To resolve this conundrum, we compared the dynamics of both the monomeric and dimeric states for each homologue at pH 6.