Effect of oxidative treatment on the secondary structure of decoloured bloodmeal

Hicks, Talia; Verbeek, Casparus Johan R.; Lay, Mark C.; Bier, James Michael

doi:10.1039/c4ra03890h

Cited by 13 publications

(20 citation statements)

References 42 publications

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“…77,82 Although it has not been reported to occur in wool exposed to hydrogen peroxide or peracetic acid, 82 it has been suggested to occur in wool exposed to boiling HP, 83 and upon bleaching hair with HP. Decolouring bloodmeal led to an increase in random structures, 37 consistent with an increase in amino acids with a propensity to form turns and coils (glycine, proline, aspartic acid and serine, despite a reduction in histidine). 77 Its presence in bloodmeal decoloured with peracetic acid is evidence that cystine cleavage occurs via C-S scission (Pathway C in Figure 7).…”

Section: Cystine Degradationmentioning

confidence: 68%

“…37 This mixture was diluted with distilled water (300 g) and immediately neutralised with 1 molL -1 sodium hydroxide and filtered. 37 This mixture was diluted with distilled water (300 g) and immediately neutralised with 1 molL -1 sodium hydroxide and filtered.…”

Section: Bloodmeal Decolouringmentioning

confidence: 99%

“…44 The generation of cysteine-S-sulfonic acid appears to be particularly pH sensitive, and its formation in acidic media may be quickly followed by its interaction with other products. 37 This highlights the difficulties of using amino acid composition alone to predict secondary structure. Sodium acetate is known to have two peaks occurring at ~ 1017 cm -1 and 1050 cm -1 , which would also be expected to increase with increasing PAA treatment due to the increase in acetic acid present which would require neutralisation.…”

Section: Cystine Degradationmentioning

confidence: 99%

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Changes to amino acid composition of bloodmeal after chemical oxidation

et al. 2015

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Bovine-derived bloodmeal can be decoloured using peracetic acid, extruded and injection moulded into a yellow translucent bioplastic. This plastic has different properties to extruded and injection moulded bloodmeal, in that it does not require sodium sulfite or urea to be extrudable. The effect of oxidation on the physical and chemical characteristics of the proteins during bloodmeal decolouring with PAA was studied by assessing changes in the amino acid profile. Polymer interactions, hydrophilicity and the destruction of cysteine crosslinks were measured indirectly by assessing protein solubility, molecular weight distribution and by synchrotron FT-IR analysis. Increasing peracetic acid concentration resulted in an increased loss of iron due to destruction of the porphyrin groups, increased solubility due to destruction or conversion of aromatic amino acids into hydrophilic groups, destruction of lysine, reduced protein content due to increased salt content in the final product, and a larger amount of smaller protein peptides but with a similar average molecular weight to bloodmeal. Amino acid analysis showed an increase in cysteine content in the product, FTIR of the sulfur groups revealed that these were heavily oxidised, such that some would be unable to participate in disulfide bonds thereby increasing protein solubility.Please do not adjust margins Please do not adjust margins conditions. The most recent investigation into the effect of PAA oxidation on dairy proteins, indicated that the amount of carbonyl groups increased while thiol (SH) groups decreased; tryptophan and methionine were most vulnerable to oxidation while lysine was not affected. 7 Neither peptide cleavage, nor

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Section: Cystine Degradationmentioning

confidence: 68%

Section: Bloodmeal Decolouringmentioning

confidence: 99%

Section: Cystine Degradationmentioning

confidence: 99%

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Changes to amino acid composition of bloodmeal after chemical oxidation

et al. 2015

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“…Toughness and increased tensile strength are associated with β-sheets in spider silk; [14,15] however, the type and extent of crystallinity can also cause materials to become brittle, while the amorphous regions provide elastomeric properties [16,17] and β-turns assist in energy storage and release. [9] Addition of SDS and TEG to decolored bloodmeal led to further changes in secondary structure composition, resulting in a more homogeneous distribution of secondary structure types throughout the bloodmeal particles. Overall, the protein contained a greater number of β-sheets after oxidation, concentrated at the core of the particle, while α-helices and random coils were found in highest concentration at the perimeter of the particles.…”

Section: Introductionmentioning

confidence: 99%

Processability and mechanical properties of bioplastics produced from decoloured bloodmeal

et al. 2017

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Bloodmeal is a protein-rich coproduct of the meat industry and can be converted into a thermoplastic. A solution of peracetic acid can be used to degrade colored compounds in bloodmeal, yielding a light yellow material. This causes an increase in β-sheets in the protein's secondary structure, but the addition of sodium dodecyl sulfate (SDS) and triethylene glycol (TEG) reduced α-helical and β-sheet content, thereby increasing random coils. Without SDS, chains were less capable of folding into these structures, preventing sufficient intermolecular interactions and chain entanglement, leading to low specific mechanical energy input (SME) during extrusion, and poor consolidation.The whiteness of molded samples showed no correlation with SME during extrusion or the degree of consolidation after extrusion; however, they were observed to have a higher level of whiteness with increasing TEG content and should be considered as a secondary process not directly linked to extrusion. Increasing the amount of water during extrusion increased the Young's modulus (E) by facilitating formation of new interactions, while increasing TEG decreased E as a result of plasticization. The action of SDS on destabilizing electrostatic and hydrophobic interactions was beneficial to extrusion, although it had no further effect during injection molding. TEG had virtually no effect on tensile strength, although it was required for flow and facilitated the formation of strong interactions after water had been evaporated during conditioning. K E Y W O R D Sbioplastics, bloodmeal, peracetic acid How to cite this article: Verbeek CJR, Low A, Lay MC, Hicks TM. Processability and mechanical properties of bioplastics produced from decolored bloodmeal.

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“…The most significant change observed as a result of decoloring bloodmeal is a major increase in chain mobility, observed as a reduction in glass transition temperature ( T g ) from ≈225 °C to around 35–45 °C . Such a drastic drop in T g is attributed to the effect of oxidation, which has led to improved chain mobility through the reduction in number and strength of stabilizing intermolecular interactions and improved chain regularity …”

Section: Introductionmentioning

confidence: 99%

The Effect of SDS and TEG on Chain Mobility and Secondary Structure of Decolored Bloodmeal

Hicks

Verbeek

Lay

et al. 2014

Macro Materials & Eng

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The effect of sodium dodecyl sulfate (SDS) and triethylene glycol (TEG) on secondary structure of decolored bloodmeal (DBM) during heating was examined via synchrotron-based Fourier transform infra-red spectroscopy (FT-IR) and wide angle X-ray scattering (WAXS). Both additives homogenize secondary structure distribution; SDS increases a-helices and decreases b-sheets and b-turns, while SDS-TEG reduces a-helices and b-sheets and increase random coils. Short heat cycles only change the composition of SDS-TEG treated DBM, implying TEG is responsible for chain mobility. Prolonged heating slowly increases b-sheets and suddenly increases a-helices at 55-75 8C in SDS-TEG treated DBM and 100 8C in SDS-treated DBM. Finally, WAXS shows that structural change due to heating is reversible for SDS-TEG treated DBM.

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Effect of oxidative treatment on the secondary structure of decoloured bloodmeal

Abstract: Synchrotron-based Fourier-transform infrared (FTIR) spectroscopy was used to assess the effect of peracetic acid decolouring on the spatial distribution of secondary structures within particles of bloodmeal.

Cited by 13 publications

References 42 publications

Changes to amino acid composition of bloodmeal after chemical oxidation

Changes to amino acid composition of bloodmeal after chemical oxidation

Processability and mechanical properties of bioplastics produced from decoloured bloodmeal

The Effect of SDS and TEG on Chain Mobility and Secondary Structure of Decolored Bloodmeal

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