Studies on egg albumen and whey protein interactions by FT-Raman spectroscopy and rheology

Ngarize, Sekai; Adams, A.R.; Howell, Nazlin K.

doi:10.1016/s0268-005x(03)00041-9

Cited by 94 publications

(67 citation statements)

References 36 publications

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“…There was no significant difference (P > 0.05) in peak intensity in the cinnamon-and cinnamaldehyde-treated samples (1.09 ± 0.024 and 1.06 ± 0.075, respectively) as compared to 0.937 ± 0.051 for BSA only ( Figure 5). Similar results were reported by Ngarize et al (2004) for heated BSA. There was a weak intensity peak at 990 cm -1 , representing the beta sheet structure (Figure 2).…”

Section: Resultssupporting

confidence: 91%

“…This decrease was attributed to the exposure of hydrophobic residues to cinnamaldehyde. A similar result was reported by Ngarize et al (2004) during the heating of BSA. Also, Badii & Howell (2002) have reported this drop in peak intensity associated with the aggregate formation of actomyosin in frozen cod and haddock.…”

Section: Resultssupporting

confidence: 90%

“…Table 1 also shows that the non-treated BSA sample's peak intensity at 990 cm -1 was 0.295 ± 0.013, which is significantly lower than those of the cinnamon and cinnamaldehyde treated BSA samples (0.423 ± 0.064 and 0.328 ± 0.053, respectively) (P < 0.05). This increase suggests the existence of anti-parallel β-pleated sheets (Ngarize et al, 2004). The absence of a peak at 1239 cm -1 was noticed (Figure 2), together with the presence of a peak at 1320 cm -1 , indicating greater helical structure content in egg albumen, in agreement with Mine et al, (1990).…”

Section: Resultssupporting

confidence: 87%

“…Also, Badii & Howell (2002) have reported this drop in peak intensity associated with the aggregate formation of actomyosin in frozen cod and haddock. This finding implies that changes in the hydrophobic environment around the aliphatic and aromatic side chains can be used to screen for denaturation and conformational changes in proteins (Ngarize et al, 2004). region for 15% BSA, 15% BSA + 500 ppm cinnamaldehyde and 15% BSA + 500 ppm cinnamon in D2O.…”

Section: Resultsmentioning

confidence: 86%

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A Study on the Effect of Cinnamon and Cinnamaldehyde on Bovine Serum Albumin (Bsa) Protein by Using Ft-Raman Spectroscopy

Alhammad¹,

Howell²

2018

JEBAS

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FT-Raman spectroscopy revealed comparative intensity changes of many bands and wave number shifts, when comparing bovine serum albumin (BSA) separately, BSA mixed with 500 ppm cinnamaldehyde and BSA mixed with 500 ppm cinnamon. It is clear that there are small shifts in wave numbers. The intensity of tryptophan band at 760 ± 2 cm -1 was 0.42 ± 0.02; there was no significant difference between the value for BSA alone and BSA + cinnamon sample (0.433 ± 0.081). In contrast, in sample BSA + cinnamaldehyde the tryptophan band intensity (0.296 ± 0.066) significantly decreased (p<0.05). The decrease was ascribed to Trp vibrational modes and C-H bending due to the enhancement of hydrophobic residues open to the outer surface of proteins. This result can be used to monitor denaturation in protein aliphatic and aromatic side chains. The decrease in the tyrosine ratio 855/830 cm -1 of the BSA mixture with cinnamon and cinnamaldehyde separately, compared to BSA alone, was attributed to strong hydrogen bonding interactions in the mixture involving tyrosine residues.

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Section: Resultssupporting

confidence: 91%

Section: Resultssupporting

confidence: 90%

Section: Resultssupporting

confidence: 87%

Section: Resultsmentioning

confidence: 86%

See 2 more Smart Citations

A Study on the Effect of Cinnamon and Cinnamaldehyde on Bovine Serum Albumin (Bsa) Protein by Using Ft-Raman Spectroscopy

Alhammad¹,

Howell²

2018

JEBAS

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“…Amide I bands often shows several components or shoulders in the region because most proteins have mixed secondary structure (Li Chan et al, 1994;Ngarize et al, 2004). In this study however, most peaks were centred around 1660 cm -1 ; there was a significant difference (p< 0.05) between chicken (3.36) and bovine (3.90) gelatin (Table 5).…”

Section: Raman Spectroscopymentioning

confidence: 48%

Preparation and characterisation of chicken skin gelatin as an alternative to mammalian gelatin

2013

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Applications of Vibrational Spectroscopy to the Analysis of Polysaccharide and Hydrocolloid Ingredients

Choi

Yuen

Phillips

et al. 2001

Handbook of Vibrational Spectroscopy

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The applications of vibrational spectroscopy to study the structure of polysaccharide and hydrocolloid ingredients are presented. Vibrational spectroscopy, including infrared (IR) and Raman spectroscopies, has been used for both qualitative and quantitative analysis of starches and other polysaccharide ingredients. Some structural characteristics of starch and nonstarch polysaccharides have been studied using various vibrational spectroscopic techniques. The degree of substitution (DS) in modified polysaccharides can also be determined by IR and Raman spectroscopy, replacing the traditional wet chemistry procedure. Vibrational spectroscopy has also been used to determine protein structural characteristics and to monitor conformational changes under different buffer conditions. Conformation is an important parameter affecting the functional properties of protein hydrocolloids, and extensive conformational changes may occur during food processing and interactions with other food ingredients. Fourier transform (FT)–mid‐IR spectroscopy has been used to obtain information on protein structure and protein–protein and protein–lipid interactions. The extent of modification in modified food proteins and the effect of these modifications on protein conformation have been monitored by Raman spectroscopy. These modified polysaccharide and protein hydrocolloids, with enhanced gelling, thickening, and emulsifying properties, are important hydrocolloid ingredients for a wide variety of food products.

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Studies on egg albumen and whey protein interactions by FT-Raman spectroscopy and rheology

Cited by 94 publications

References 36 publications

A Study on the Effect of Cinnamon and Cinnamaldehyde on Bovine Serum Albumin (Bsa) Protein by Using Ft-Raman Spectroscopy

A Study on the Effect of Cinnamon and Cinnamaldehyde on Bovine Serum Albumin (Bsa) Protein by Using Ft-Raman Spectroscopy

Preparation and characterisation of chicken skin gelatin as an alternative to mammalian gelatin

Applications of Vibrational Spectroscopy to the Analysis of Polysaccharide and Hydrocolloid Ingredients

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