Fingerprints mass spectrometry

N. (2004) Maturity discrimination of snake frmt (Salacca edulis Reinw.) cv. Pondoh based on volatiles analysis using an electronic nose device eqmpped with a sensor array and fingerprint mass spectrometry. Flavour Fragrance J. 19 44-50. 

Kojima, H., Araki, S., Kaneda, H., Takashio, M. (2005) Application of a new electronic nose with fingerprinting mass spectrometry to brewing. J. Am. Soc. Brew. Chem. 63 151-156. 

Biasioli,F, Gasperi,F, Aprea, E., Colato, L., Boscaini, E., Mark, T.D. (2003) Fingerprinting mass spectrometry by PTR-MS heat treatment vs. pressure treatment of red orange juice—a case study. International Journal of Mass Spectrometry, 223, 343-353. 

High performance spectroscopic methods, like FT-IR and NIR spectrometry and Raman spectroscopy are widely applied to identify non-destructively the specific fingerprint of an extract or check the stability of pure molecules or mixtures by the recognition of different functional groups. Generally, the infrared techniques are more frequently applied in food colorant analysis, as recently reviewed. Mass spectrometry is used as well, either coupled to HPLC for the detection of separated molecules or for the identification of a fingerprint based on fragmentation patterns. ... 

To identify the volatile components, gas chromatography-mass spectrometry (GC-MS) is still the method of choice. A comparison of the GC fingerprints of B. carter a and B. serrata reveals the different composition of the volatile fractions (Figure 16.1). Common monoterpenes, aliphatic, and aromatic compounds of olibanum are, e g., pinene, limonene, 1,8-cineole, bomyl acetate, and methyleugenol (Figure 16.2). 

Chambery, A., del Monaco, G., Di Maro, A., and Parente, A. (2009). Peptide fingerprint of high quality Campania white wines by MALDl-TOP mass spectrometry. Food Chem. 113, 1283-1289. 

Figure 2.4. Peptide fingerprinting by MALDI-TOF mass Spectrometry. Proteins are extracted and separated on by 2D gel electrophoresis. A spot of interest is excised from the gel, digested with trypsin, and ionized by MALDI. The precise mass of proteolytic fragments is determined by time-of- flight mass spectrometry. The identity of the protein is determined by comparing the peptide masses with a list of peptide masses generated by a simulated digestion of all of the open reading frames of the organism.

The major advantage of the tandem mass spectrometry approach compared to MALDI peptide fingerprinting, is that the sequence information obtained from the peptides is more specific for the identification of a protein than simply determining the mass of the peptides. This permits a search of expressed sequence tag nucleotide databases to discover new human genes based upon identification of the protein. This is a useful approach because, by definition, the genes identified actually express a protein. 

Arnold, R. J. Reilly, J. P. Fingerprint matching of E. coli strains with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry of whole cells using a modified correlation approach. Rapid Commun. Mass Spectrom. 1998,12,630-636. 

Woolfitt, A. Moura, H. Barr, J. De, B. Popovic,T. Satten, G. Jarman, K. H. Wahl, K. L., Differentiation of Bacillus spp. by MALDI-TOF mass spectrometry using a bacterial fingerprinting algorithm and a random forest classification algorithm. Presented at 5th ISIAM Meeting, Richland, WA 2004. 

Different strains of E. coli have unique fingerprints when analyzed by MALDI mass spectrometry of whole cells, as illustrated by the spectra of Figure 9.3. Many peaks appear at the same masses in all of the spectra, with only modest intensity variations. A few peaks also vary dramatically in intensity for these four strains. We expect the spectra to be similar, since all the strains are laboratory derivatives of the single E. coli strain, K-12. Genetic modifications can, and most likely do, affect biological functions such as tran-... 

Variations on the spectral peaks from different species of the same genus were also observed. Three species of Pseudomonas produced the spectra shown in Figure 14.2. These spectra are clearly unique and were used to correctly identify unknown samples. Because of peak ratio reproducibility issues in bacterial protein profiles obtained by MALDI MS,11 a fingerprint approach that had been used for other mass spectrometry approaches has not been used. The profile reproducibility problem was first recognized by Reilly et al.12,13 and later researched by others in the field.14,15 As a later alternative, a direct comparison of the mass-to-charge ratio (m/z) of the unknown mass spectral peaks with a database of known protein masses has been used to identify unknown samples.14... 

With recent developments in analytical instrumentation these criteria are being increasingly fulfilled by physicochemical spectroscopic approaches, often referred to as whole-organism fingerprinting methods.910 Such methods involve the concurrent measurement of large numbers of spectral characters that together reflect the overall cell composition. Examples of the most popular methods used in the 20th century include pyrolysis mass spectrometry (PyMS),11,12 Fourier transform-infrared spectrometry (FT-IR), and UV resonance Raman spectroscopy.16,17 The PyMS technique... 

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