2006
DOI: 10.1016/j.idairyj.2005.06.007
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Mapping of ice cream formulation using front-face fluorescence spectroscopy

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Cited by 15 publications
(8 citation statements)
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“…Front-face fluorescence spectroscopy is based on obtaining emission spectra of tryptophan from which it can be deduced whether the protein tryptophan residues are in a hydrophilic or hydrophobic environment. , Emission spectra in the range of 310–380 nm were fitted to Gaussian distributions, and the wavelengths of the peak positions (λ max ) were registered. A plot of λ max against the concentration of caseinate in the serum obtained by centrifugation on day 0 gave a linear correlation for emulsions with LACTEM and GMS (Figure ), showing high concentration of caseinate in aqueous serum corresponded to high λ max .…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…Front-face fluorescence spectroscopy is based on obtaining emission spectra of tryptophan from which it can be deduced whether the protein tryptophan residues are in a hydrophilic or hydrophobic environment. , Emission spectra in the range of 310–380 nm were fitted to Gaussian distributions, and the wavelengths of the peak positions (λ max ) were registered. A plot of λ max against the concentration of caseinate in the serum obtained by centrifugation on day 0 gave a linear correlation for emulsions with LACTEM and GMS (Figure ), showing high concentration of caseinate in aqueous serum corresponded to high λ max .…”
Section: Resultsmentioning
confidence: 99%
“…It has also been established that tryptophan in hydrophilic and hydrophobic environments yields peaks in emission spectra at 333 and 319 nm, respectively. 33,34 A larger proportion in hydrophilic environment would consequently shift λ max to a higher value. The firm emulsions containing 0.3− 1.0 wt % GMU diverged from the linear correlation (Figure 4).…”
Section: Stability and Rheologicalmentioning
confidence: 99%
“…Front face fluorescence was performed on ice cream preparations for their characterization. The spectra were taken in the tryptophan region (excitation 290 nm emission 300–360 nm) and principal component analysis and discriminant analysis (PCA‐DA) as well as PLS‐DA were performed to reach a clear discrimination of protein and fat by their type and source in different ice cream formulations 87.…”
Section: Fluorescence Spectroscopymentioning
confidence: 99%
“…Die Spektren wurden im Bereich der Tryptophan‐Emission (300 – 360 nm, Anregung 290 nm) gemessen. Um eine klare Unterscheidung von Eiscremerezepturen mit Proteinen und Fetten verschiedener Art und Herkunft zu ermöglichen, wurden die PCA‐ und die PLS‐Diskriminanzanalyse zur Auswertung herangezogen 84.…”
Section: Fluoreszenz‐spektroskopieunclassified