Background: Collagen hydrolysates (CH) in functional foods and supplements are dietary sources of amino acids (AAs) and di-and tripeptides linked to various health benefits. This study aimed to investigate the single-dose bioavailability of skin- and hide-derived CH from fish, porcine and bovine origin with different molecular weights (bovine 2,000 and 5,000 Da).
Methods: A randomized, double-blind crossover clinical study was performed with healthy volunteers assessing the plasma concentration of free and peptide-bound hydroxyproline (Hyp) as well as selected peptides reported to be abundantly present in collagen.
There are various analytical techniques available to address the growing interest in the composition of food products. LC-HRMS(/MS) is the most comprehensive technique, providing detailed information at the molecular level. However, given the vast number of different molecules encountered in food products, it is important to obtain a global overview of the dataset before focusing on similarities and differences.
View Article and Find Full Text PDFIt can be important for consumers to know whether food products contain animal material and, if so, of which species. Food products with animal material as an ingredient often contain collagen type 1. LC-MS/MS (Liquid Chromatography-tandem Mass Spectrometry) was applied as technique to generically detect bird.
View Article and Find Full Text PDFIn contrast to collagens 1α1 and 1α2, the more obscure collagen 1α3 is sparsely mentioned in literature. In skin collagen type 1 of teleosts (bony fish), however, the chain occurs in a heterotrimer together with collagens 1α1 and 1α2, which makes it one of the most abundant proteins in teleosts. As teleost fish species and gelatin (hydrolysate) prepared from their skin are a major source for food products and nutraceuticals, the goal of the study was to selectively identify collagen 1α3 in several fish species.
View Article and Find Full Text PDFHemolysis can result in analyte suppression or enhancement and it can affect the extraction efficiency and analyte stability. Triskelion developed an LC-MSÂ method to monitor hemolysis. The concept can be integrated into existing and new quantitative protein LC-MS methods and can be validated according to the most appropriate tier.
View Article and Find Full Text PDFRationale: It is important to investigate the behavior of protein hydrolysate components in both in vitro and in vivo studies, to support the elucidation of their biological functions. As protein hydrolysates and biological matrices are highly complex mixtures, it is essential to apply fully reliable and flexible analytical approaches.
Methods: A novel and generic Liquid Chromatography/Mass Spectrometry methodology was developed to analyze short peptides.
Protein hydrolysates are an important part of the human diet. Often, they are prepared from milk, soy, or collagen. In the present study, four different collagen hydrolysates were tested, varying in the average molecular weight and the animal source.
View Article and Find Full Text PDFCollagen is an important structural protein and the most abundant protein in mammals. In several research fields, structural analysis of collagens is performed. Fibrillar collagens almost entirely consist of continuous repeats of GXY, where G is glycine, X is often proline or alanine and Y is often hydroxyproline or alanine.
View Article and Find Full Text PDFCollagen is the most abundant protein family in mammals. Commercial edible gelatins are often produced from bovine and porcine skin and bone and consist mainly of partially hydrolyzed collagen type 1. The gelatin industry would benefit from a sensitive and reliable species detection method to unambiguously demonstrate species authenticity of their products.
View Article and Find Full Text PDFBackground: TNO Triskelion has applied its general workflow for the development of quantitative LC-MS methods for proteins in biological matrices to the quantification of infliximab in rat serum using bottom up μLC-MS/MS. Results/methodology: The general workflow consists of sample purification, analyte processing and LC-MS analysis. In the development of a quantitative μLC-MS/MS method for infliximab in rat serum the analyte processing part and the LC-MS part were optimized, in order to meet the different sample requirements of μLC-MS as compared with UPLC-MS.
View Article and Find Full Text PDFPenicillins are used universally in both human and veterinary medicine. The European Union (EU) has established maximum residue levels (MRLs) for most ss-lactam antibiotics in milk and animal tissues and included them in the National Residue Monitoring Programs. In this study, a novel method is described for the determination and confirmation of eight penicillins in porcine tissues, milk and animal feed by liquid chromatography-tandem mass spectrometry (LC-MS/MS).
View Article and Find Full Text PDFAminoglycosides (AGs) are a large and diverse group of antibiotics. Although AGs may cause side effects of nephrotoxicity and ototoxicity, they are still occasionally being used for the treatment of serious infections. In this study the development of a method is described for the quantitative determination and confirmation of seven aminoglycosides (and relevant isomers) and spectinomycin in animal tissues.
View Article and Find Full Text PDFAn improved comprehensive two-dimensional (LC x LC) HPLC system for the analysis of triacylglycerols was developed. In the first-dimension, a Ag(I)-coated cation exchanger (250 mm x 2.1 mm, 5 microm) was employed with a gradient from 100% MeOH to 6% MeCN in MeOH at 20 microL/min.
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