The desalting process is critical for packaging table olives in brine with reduced NaCl or fortified mineral nutrients. In this study, the effect of desalting on the physicochemical characteristics and mineral content of green Manzanilla Spanish-style (plain and stuffed with pepper paste) and DOP table olives was investigated for the first time. The surface colour of the fruits turned slightly brownish, and the olives became somewhat softer. The lactic acid, the mineral macronutrients (mainly) and micronutrient contents decreased, while flesh moisture increased. The kinetic parameters of the minerals' losses depended on the presentation, with the estimated values for plain olives being the lowest (slowest desalting). Overall, the desalting process resulted in slight quality damage and a moderated decrease in the mineral concentration in the flesh, leading to some product degradation. This study provides quantitative information on these changes that may affect the commercial value of the final products and offers information for viable designs.
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http://dx.doi.org/10.3390/foods12122307 | DOI Listing |
Anal Chem
January 2025
Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, United States.
Intact protein analysis using mass spectrometry (MS) is an important technique to characterize and provide a comprehensive overview of protein complexity. It is also the basis of "top-down" approaches in proteomics to describe the proteoforms of single protein's post-translational modifications (PTMs). MS-based analysis of intact proteins benefits from high-resolution separations prior to electrospray ionization.
View Article and Find Full Text PDFMethods Mol Biol
December 2024
Department of Biochemistry, Center for Biomedical Mass Spectrometry, Boston University School of Medicine, Boston, MA, USA.
Mass spectrometry-based investigation of the heterogeneous glycoproteome from complex biological specimens is a robust approach to mapping the structure, function, and dynamics of the glycome and proteome. Sampling whole wet tissues often provides a large amount of starting material; however, there is a reasonable variability in tissue handling prior to downstream processing steps, and it is difficult to capture all the different biomolecules from a specific region. The on-slide tissue digestion approach, outlined in this protocol chapter, is a simple and cost-effective method that allows comprehensive mapping of the glycoproteome from a single spot of tissue of 1 mm or greater diameter.
View Article and Find Full Text PDFMethods Mol Biol
December 2024
Department of Biological Sciences, University of the Pacific, Stockton, CA, USA.
Adipose tissue (AT) is a complex, multifunctional endocrine organ that plays a significant role in animal evolution and human disease. Profiling of the proteome, or the set of proteins produced by a cell or tissue at a given time, can be used to explore the myriad functions of adipose tissue and understand its role in health and disease. The main challenges of adipose tissue proteomics include the high lipid and low protein content of the tissue and association of many proteins with lipid droplets.
View Article and Find Full Text PDFMass Spectrom Rev
December 2024
Department of Chemistry and Chemical Biology, Indiana University, Indianapolis, Indiana, USA.
Mass spectrometry (MS) is a powerful analytical technique that typically involves sample preparation and online analytical separation before MS detection. Traditional methods often face bottlenecks in sample preparation and analytical separation, despite the rapid detection capabilities of MS. This review explores the integration of electrokinetic manipulations directly with the ionization step to enhance MS performance, focusing on methods that eliminate or simplify sample preparation and separation processes.
View Article and Find Full Text PDFSLAS Discov
December 2024
Department of Cancer Biology and the Linde Program in Cancer Chemical Biology, Dana-Farber Cancer Institute, Boston, MA, USA; Blais Proteomics Center, Dana-Farber Cancer Institute, Boston, MA, USA; Center for Emergent Drug Targets, Dana-Farber Cancer Institute, Boston, MA, USA; Department of Pathology, Brigham and Women's Hospital and Harvard Medical School, Boston, MA, USA. Electronic address:
Target-based screening of covalent fragment libraries with mass spectrometry has emerged as a powerful strategy to identify chemical starting points for small molecule inhibitors or find new binding pockets on proteins of interest. These libraries span diverse chemical space with a modest number of compounds. Screening covalent fragments against purified protein targets reduces the demands on the mass spectrometer with respect to absolute throughput, detection limit, and dynamic range.
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