Impact of urea on the microstructure of commercial canola protein–carrageenan network: A research note

Uruakpa, F.O.; Arntfield, Susan D.

doi:10.1016/j.ijbiomac.2006.01.016

Cited by 23 publications

(8 citation statements)

References 11 publications

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“…The reducing effects of NaHSO 3 on protein can break the disulfide linkage and dissociate the protein into smaller polypeptide chains, and a concentration of 15 g/L was apparently needed to break completely the disulfide bonds in napin. The reducing effects of NaHSO 3 could also be reflected by the attenuated bands at 55 kDa, belonging to the cruciferin subunits stabilized by disulfide bonds, and the intense bands at 30 kDa, belonging to the disassociated polypeptides [24].…”

Section: Sds-pagementioning

confidence: 99%

Physicochemical Properties and Adhesion Performance of Canola Protein Modified with Sodium Bisulfite

Sun

et al. 2011

J Americ Oil Chem Soc

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The objective of this research was to study the adhesion properties of sodium bisulfite (NaHSO 3 )-modified canola protein. Protein was extracted from canola meal through alkali solubilization and acid precipitation methods, then modified with different concentrations of NaHSO 3 (0-15 g/L) during the isolation process. As NaHSO 3 concentration increased, canola protein purities decreased. Amino acid profiles showed that the hydrophobic amino acids in canola protein constituted only 27% of total protein, indicating that canola protein is mostly hydrophilic. The reducing effects of NaHSO 3 were exerted on canola protein through the breaking of disulfide bonds in both its cruciferin and napin components, as reflected by the protein electrophoresis profile, DSC data, and morphological images. The wet protein isolates were used as adhesives. The greatest wet shear strength of canola protein adhesive without modification was 3.97 MPa with 100% wood cohesive failure (WCF), observed at a curing temperature of 190°C. NaHSO 3 had slight weakening effects on the adhesion performance of canola protein. Canola protein modified with 3 g/L NaHSO 3 exhibited wet shear strength similar to the control at 190°C and higher strength at 150 and 170°C. The NaHSO 3 modification significantly improved handling and flowability of canola protein adhesives.

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Section: Sds-pagementioning

confidence: 99%

Physicochemical Properties and Adhesion Performance of Canola Protein Modified with Sodium Bisulfite

Sun

et al. 2011

J Americ Oil Chem Soc

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“…The method is suitable for measurement of subtle changes associated with gel forming phenomena (Hamann, 1987). High G 0 (storage modulus) values demonstrate a stronger intermolecular network and increased interactions between protein-protein and proteinpolysaccharide molecules, while low tan d values indicate a more elastic network (Uruakpa & Arntfield, 2006).…”

Section: Introductionmentioning

confidence: 99%

Gelation properties of salt-extracted pea protein induced by heat treatment

Sun

Arntfield

2010

Food Research International

226

120

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“…The method is suitable for following subtle changes associated with gel forming phenomenon (Hamann, 1987). High G 0 (storage modulus) values are indicative of stronger intermolecular network and increased interactions between proteins, while low tan d values indicate a more elastic network (Uruakpa & Arntfield, 2006).…”

Section: Introductionmentioning

confidence: 99%

Gelation properties of salt-extracted pea protein isolate induced by heat treatment: Effect of heating and cooling rate

Sun

Arntfield

2011

Food Chemistry

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Impact of urea on the microstructure of commercial canola protein–carrageenan network: A research note

Cited by 23 publications

References 11 publications

Physicochemical Properties and Adhesion Performance of Canola Protein Modified with Sodium Bisulfite

Physicochemical Properties and Adhesion Performance of Canola Protein Modified with Sodium Bisulfite

Gelation properties of salt-extracted pea protein induced by heat treatment

Gelation properties of salt-extracted pea protein isolate induced by heat treatment: Effect of heating and cooling rate

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