全部 标题 作者
关键词 摘要

OALib Journal期刊
ISSN: 2333-9721
费用:99美元

查看量下载量

相关文章

更多...

Fluorescence Rejection by Shifted Excitation Raman Difference Spectroscopy at Multiple Wavelengths for the Investigation of Biological Samples

DOI: 10.5402/2012/256326

Full-Text   Cite this paper   Add to My Lib

Abstract:

Shifted excitation Raman difference spectroscopy (SERDS) was applied for an effective fluorescence removal in the Raman spectra of meat, fat, connective tissue, and bone from pork and beef. As excitation light sources, microsystem diode lasers emitting at 783?nm, 671?nm, and 488?nm each incorporating two slightly shifted excitation wavelengths with a spectral difference of about 10?cm?1 necessary for SERDS operation were used. The moderate fluorescence interference for 783?nm excitation as well as the increased background level at 671?nm was efficiently rejected using SERDS resulting in a straight horizontal baseline. This allows for identification of all characteristic Raman signals including weak bands which are clearly visible and overlapping signals that are resolved in the SERDS spectra. At 488?nm excitation, the spectra contain an overwhelming fluorescence interference masking nearly all Raman signals of the probed tissue samples. However, the essentially background-free SERDS spectra enable determining the majority of characteristic Raman bands of the samples under investigation. Furthermore, 488?nm excitation reveals prominent carotenoid signals enhanced due to resonance Raman scattering which are present in the beef samples but absent in pork tissue enabling a rapid meat species differentiation. 1. Introduction Due to its fingerprinting characteristics, Raman spectroscopy is well suited for the investigation of biological material, for example, for rapid and nondestructive identification purposes. Here, excitation wavelengths in the visible or near-infrared range are preferable to avoid strong absorption of water leading to sample heating [1]. For that reason, in situ Raman investigations are possible since no sample pretreatments, as for example, drying procedures, are necessary. According to the λ?4-dependence of the Raman scattering intensity, the application of shorter excitation wavelengths can significantly improve the spectral quality. On the other hand, this leads to an increased fluorescence interference partly or completely obscuring the Raman signals and thus making the detection of useful spectra hardly possible. There exist certain methods to remove the fluorescence background from the Raman spectra to overcome the fluorescence issue. In that way, mathematical approaches as polynomial [2] or advanced subtraction methods [3] as well as experimental techniques using a temporal discrimination of the slower fluorescence emission against the Raman photons [4, 5] were successfully applied. As a technique additionally removing the

References

[1]  N. A. Marigheto, E. K. Kemsley, J. Potter, P. S. Belton, and R. H. Wilson, “Effects of sample heating in FT-Raman spectra of biological materials,” Spectrochimica Acta A, vol. 52, no. 12, pp. 1571–1579, 1996.
[2]  C. A. Lieber and A. Mahadevan-Jansen, “Automated method for subtraction of fluorescence from biological raman spectra,” Applied Spectroscopy, vol. 57, no. 11, pp. 1363–1367, 2003.
[3]  Z. M. Zhang, S. Chen, Y. Z. Liang et al., “An intelligent background-correction algorithm for highly fluorescent samples in Raman spectroscopy,” Journal of Raman Spectroscopy, vol. 41, no. 6, pp. 659–669, 2010.
[4]  N. Everall, T. Hahn, P. Matousek, A. W. Parker, and M. Towrie, “Picosecond time-resolved Raman spectroscopy of solids: capabilities and limitations for fluorescence rejection and the influence of diffuse reflectance,” Applied Spectroscopy, vol. 55, no. 12, pp. 1701–1708, 2001.
[5]  E. V. Efremov, J. B. Buijs, C. Gooijer, and F. Ariese, “Fluorescence rejection in resonance Raman spectroscopy using a picosecond-gated intensified charge-coupled device camera,” Applied Spectroscopy, vol. 61, no. 6, pp. 571–578, 2007.
[6]  A. P. Shreve, N. J. Cherepy, and R. A. Mathies, “Effective rejection of fluorescence interference in Raman spectroscopy using a shifted excitation difference technique,” Applied Spectroscopy, vol. 46, no. 4, pp. 707–711, 1992.
[7]  J. Zhao, M. M. Carrabba, and F. S. Allen, “Automated fluorescence rejection using shifted excitation Raman difference spectroscopy,” Applied Spectroscopy, vol. 56, no. 7, pp. 834–845, 2002.
[8]  M. A. da Silva Martins, D. G. Ribeiro, E. A. Pereira dos Santos, A. A. Martin, A. Fontes, and H. da Silva Martinho, “Shifted-excitation Raman difference spectroscopy for in vitro and in vivo biological samples analysis,” Biomedical Optics Express, vol. 1, no. 2, pp. 617–626, 2010.
[9]  H. Schmidt, K. Sowoidnich, M. Maiwald, B. Sumpf, and H. D. Kronfeldt, “Hand-held Raman sensor head for in-situ characterization of meat quality applying a microsystem 671?nm diode laser,” in Advanced Environmental, Chemical, and Biological Sensing Technologies VI, vol. 7312 of Proceedings of SPIE, pp. 73120H-1–73120H-8, Orlando, Fla, USA, April 2009.
[10]  H. Wenzel, A. Klehr, M. Braun et al., “High-power 783?nm distributed-feedback laser,” Electronics Letters, vol. 40, no. 2, pp. 123–124, 2004.
[11]  M. Maiwald, G. Erbert, A. Klehr et al., “Rapid shifted excitation Raman difference spectroscopy with a distributed feedback diode laser emitting at 785?nm,” Applied Physics B, vol. 85, no. 4, pp. 509–512, 2006.
[12]  H. Schmidt, K. Sowoidnich, and H. D. Kronfeldt, “A prototype hand-held raman sensor for the in situ characterization of meat quality,” Applied Spectroscopy, vol. 64, no. 8, pp. 888–894, 2010.
[13]  C. K. Johnson and R. Rubinovitz, “Near-infrared excitation of Raman scattering by chromophoric proteins,” Spectrochimica Acta A, vol. 47, no. 9-10, pp. 1413–1421, 1991.
[14]  V. Palaniappan and D. F. Bocian, “Acid-induced transformations of myoglobin. Characterization of a new equilibrium heme-pocket intermediate,” Biochemistry, vol. 33, no. 47, pp. 14264–14274, 1994.
[15]  U. B?cker, R. Ofstad, Z. Wu et al., “Revealing covariance structures in fourier transform infrared and Raman microspectroscopy spectra: a study on pork muscle fiber tissue subjected to different processing parameters,” Applied Spectroscopy, vol. 61, no. 10, pp. 1032–1039, 2007.
[16]  A. M. Herrero, “Raman spectroscopy for monitoring protein structure in muscle food systems,” Critical Reviews in Food Science and Nutrition, vol. 48, no. 6, pp. 512–523, 2008.
[17]  R. Tuma, “Raman spectroscopy of proteins: from peptides to large assemblies,” Journal of Raman Spectroscopy, vol. 36, no. 4, pp. 307–319, 2005.
[18]  M. Bouraoui, S. Nakai, and E. Li-Chan, “In situ investigation of protein structure in Pacific whiting surimi and gels using Raman spectroscopy,” Food Research International, vol. 30, no. 1, pp. 65–72, 1997.
[19]  E. B. Carew, I. M. Asher, and H. E. Stanley, “Laser Raman spectroscopy—new probe of myosin substructure,” Science, vol. 188, no. 4191, pp. 933–936, 1975.
[20]  S. P. Verma, J. R. Philippot, B. Bonnet, J. Sainte-Marie, Y. Moschetto, and D. F. H. Wallach, “Raman studies of structural rearrangements induced in human plasma lipoprotein carotenoids by malondialdehyde,” Lipids, vol. 20, no. 12, pp. 890–896, 1985.
[21]  V. E. de Oliveira, H. V. Castro, H. G. M. Edwards, and L. F. C. de Oliveiraa, “Carotenes and carotenoids in natural biological samples: a Raman spectroscopic analysis,” Journal of Raman Spectroscopy, vol. 41, no. 6, pp. 642–650, 2010.
[22]  M. Careche, A. M. Herrero, A. Rodriguez-Casado, M. L. Del Mazo, and P. Carmona, “Structural changes of hake (Merluccius merluccius L.) fillets: effects of freezing and frozen storage,” Journal of Agricultural and Food Chemistry, vol. 47, no. 3, pp. 952–959, 1999.
[23]  J. W. Chan, D. Motton, J. C. Rutledge, N. L. Keim, and T. Huser, “Raman spectroscopic analysis of biochemical changes in individual triglyceride-rich lipoproteins in the pre- and postprandial state,” Analytical Chemistry, vol. 77, no. 18, pp. 5870–5876, 2005.
[24]  J. R. Beattie, S. E. J. Bell, C. Borgaard, A. Fearon, and B. W. Moss, “Prediction of adipose tissue composition using Raman spectroscopy: average properties and individual fatty acids,” Lipids, vol. 41, no. 3, pp. 287–294, 2006.
[25]  L. B. Lyndgaard, K. M. S?rensen, F. van den Berg, and S. B. Engelsen, “Depth profiling of porcine adipose tissue by Raman spectroscopy,” Journal of Raman Spectroscopy, vol. 43, no. 4, pp. 482–489, 2012.
[26]  E. F. Olsen, C. Baustad, B. Egelandsdal, E.-O. Rukke, and T. Isaksson, “Long-term stability of a Raman instrument determining iodine value in pork adipose tissue,” Meat Science, vol. 85, no. 1, pp. 1–6, 2010.
[27]  E. F. Olsen, E.-O. Rukke, B. Egelandsdal, and T. Isaksson, “Determination of omega-6 and omega-3 fatty acids in pork adipose tissue with nondestructive raman and fourier transform infrared spectroscopy,” Applied Spectroscopy, vol. 62, no. 9, pp. 968–974, 2008.
[28]  E. F. Olsen, E.-O. Rukke, A. Fl?tten, and T. Isaksson, “Quantitative determination of saturated-, monounsaturated- and polyunsaturated fatty acids in pork adipose tissue with non-destructive Raman spectroscopy,” Meat Science, vol. 76, no. 4, pp. 628–634, 2007.
[29]  S. P. Verma and D. F. H. Wallach, “Raman spectra of some saturated, unsaturated and deuterated c18 fatty acids in the HCH deformation and CH stretching regions,” Biochimica et Biophysica Acta, vol. 486, no. 2, pp. 217–227, 1977.
[30]  A. Tfayli, O. Piot, F. Draux, F. Pitre, and M. Manfait, “Molecular characterization of reconstructed skin model by Raman microspectroscopy: comparison with excised human skin,” Biopolymers, vol. 87, no. 4, pp. 261–274, 2007.
[31]  T. Ikoma, H. Kobayashi, J. Tanaka, D. Walsh, and S. Mann, “Physical properties of type I collagen extracted from fish scales of Pagrus major and Oreochromis niloticas,” International Journal of Biological Macromolecules, vol. 32, no. 3–5, pp. 199–204, 2003.
[32]  V. A. Iconomidou, M. E. Georgaka, G. D. Chryssikos, V. Gionis, P. Megalofonou, and S. J. Hamodrakas, “Dogfish egg case structural studies by ATR FT-IR and FT-Raman spectroscopy,” International Journal of Biological Macromolecules, vol. 41, no. 1, pp. 102–108, 2007.
[33]  B. G. Frushour and J. L. Koenig, “Raman scattering of collagen, gelatin, and elastin,” Biopolymers, vol. 14, no. 2, pp. 379–391, 1975.
[34]  H. G. M. Edwards, D. W. Farwell, J. M. Holder, and E. E. Lawson, “Fourier-transform Raman spectroscopy of ivory: II. Spectroscopic analysis and assignments,” Journal of Molecular Structure, vol. 435, no. 1, pp. 49–58, 1997.
[35]  J. Chen, C. Burger, C. V. Krishnan, B. Chu, B. S. Hsiao, and M. J. Glimcher, “In vitro mineralization of collagen in demineralized fish bone,” Macromolecular Chemistry and Physics, vol. 206, no. 1, pp. 43–51, 2005.
[36]  S. Jaisson, S. Lorimier, S. Ricard-Blum et al., “Impact of carbamylation on type I collagen conformational structure and its ability to activate human polymorphonuclear neutrophils,” Chemistry and Biology, vol. 13, no. 2, pp. 149–159, 2006.
[37]  M. D. Morris and W. F. Finney, “Recent developments in Raman and infrared spectroscopy and imaging of bone tissue,” Spectroscopy, vol. 18, no. 2, pp. 155–159, 2004.
[38]  S. Le Blond, E. Guilminot, G. Lemoine, N. Huet, and J. Y. Mevellec, “FT-Raman spectroscopy: a positive means of evaluating the impact of whale bone preservation treatment,” Vibrational Spectroscopy, vol. 51, no. 2, pp. 156–161, 2009.
[39]  J. A. Timlin, A. Carden, M. D. Morris, R. M. Rajachar, and D. H. Kohn, “Raman spectroscopic imaging markers for fatigue-related microdamage in bovine bone,” Analytical Chemistry, vol. 72, no. 10, pp. 2229–2236, 2000.
[40]  G. McLaughlin and I. K. Lednev, “Spectroscopic discrimination of bone samples from various species,” American Journal of Analytical Chemistry, vol. 3, no. 2, pp. 161–167, 2012.
[41]  G. Penel, G. Leroy, C. Rey, and E. Bres, “MicroRaman spectral study of the PO4 and CO3 vibrational modes in synthetic and biological apatites,” Calcified Tissue International, vol. 63, no. 6, pp. 475–481, 1998.
[42]  M. Maiwald, H. Schmidt, B. Sumpf, G. Erbert, H. D. Kronfeldt, and G. Tr?nkle, “Microsystem 671nm light source for shifted excitation Raman difference spectroscopy,” Applied Optics, vol. 48, no. 15, pp. 2789–2792, 2009.
[43]  M. Maiwald, H. Schmidt, B. Sumpf et al., “Microsystem light source at 488?nm for shifted excitation resonance Raman difference spectroscopy,” Applied Spectroscopy, vol. 63, no. 11, pp. 1283–1287, 2009.
[44]  H. Schmidt, D. Pérez-Kaiser, and M. Maiwald, “Method for generating and for detecting a Raman spectrum,” International Patent WO, 2011/033017 A1, 2011.

Full-Text

Contact Us

service@oalib.com

QQ:3279437679

WhatsApp +8615387084133