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dc.contributor.author
Schwaighofer, Andreas
dc.contributor.author
Alcaraz, Mirta Raquel
dc.contributor.author
Kuligowski, Julia
dc.contributor.author
Lendl, Bernhard
dc.date.available
2019-11-12T17:27:23Z
dc.date.issued
2018-01
dc.identifier.citation
Schwaighofer, Andreas; Alcaraz, Mirta Raquel; Kuligowski, Julia; Lendl, Bernhard; Recent advancements of EC-QCL based mid-IR transmission spectroscopy of proteins and application to analysis of bovine milk; IOS Press; Biomedical Spectroscopy and Imaging; 7; 1-2018; 35-45
dc.identifier.issn
2212-8794
dc.identifier.uri
http://hdl.handle.net/11336/88641
dc.description.abstract
Background:High emission powers of external cavity-quantum cascade laser (EC-QCL) light sources allow to employ significantly larger path lengths for infrared (IR) transmission measurements compared to conventional Fourier-transform infrared (FTIR) measurements employing thermal emitters. Objective:An EC-QCL based IR transmission setup is presented as a viable alternative for analysis of proteins in both, academic protein structure studies as well as in process analytical applications. Here, the application of EC-QCL based IR transmission spectroscopy is introduced for i) monitoring of the protein secondary structure and ii) rapid screening of the thermal history of commercial milk samples without prior sample preparation. Methods:Proteins present in milk were measured by QCL-IR and FTIR spectroscopy and spectra were compared. Dynamic conformational changes were followed by QCL-IR spectroscopy after chemical denaturation. Sixteen commercial milk samples were surveyed by QCL-IR spectroscopy and classified according to the experienced heat load during processing. Results:The 4?5 times higher applicable transmission path length (38 μm for QCL vs. 8 μm for FTIR measurements) allows robust measurements of the protein amide I band in aqueous solutions. It was shown that IR spectra of the protein amide I band acquired by EC-QCL transmission spectroscopy are comparable to FTIR spectra and the acquired spectra were employed for the study of conformational changes in protein standard solutions. Furthermore, a classification analysis of commercial bovine milk samples based on their thermal history was accomplished. Conclusions:The potential application of EC-QCL IR spectroscopy was demonstrated as a tool for following conformational changes of the secondary protein structure as well as for fast screening for estimating the heat load applied to commercial milk.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
IOS Press
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
QUANTUM CASCADE LASER
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IR SPECTROSCOPY
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PROTEIN SECONDARY STRUCTURE
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MILK ANALYSIS
dc.subject.classification
Química Analítica
dc.subject.classification
Ciencias Químicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Recent advancements of EC-QCL based mid-IR transmission spectroscopy of proteins and application to analysis of bovine milk
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-10-16T15:24:40Z
dc.identifier.eissn
2212-8808
dc.journal.volume
7
dc.journal.pagination
35-45
dc.journal.pais
Países Bajos
dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Schwaighofer, Andreas. Technische Universitat Wien; Austria
dc.description.fil
Fil: Alcaraz, Mirta Raquel. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Química. Cátedra de Química Analítica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
dc.description.fil
Fil: Kuligowski, Julia. Health Research Institute La Fe; España. University Of Natural Resources And Life Sciences; Austria
dc.description.fil
Fil: Lendl, Bernhard. Technische Universitat Wien; Austria
dc.journal.title
Biomedical Spectroscopy and Imaging
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://content.iospress.com/articles/biomedical-spectroscopy-and-imaging/bsi177
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.3233/BSI-180177
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