Properties of a Soluble Form of High-Pressure-Treated Egg Albumen

Iametti, Stefania; Donnizzelli, E.; Pittia, Paola; Rovere, P.; Squarcina, N.; Bonomi, Francesco

doi:10.1007/978-3-642-60196-5_69

Cited by 3 publications

(4 citation statements)

References 4 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We had no evidence for a transient change in catalytic activity under pressure for either enzyme when pressure-treated in the presence of synthetic substrates (not shown). All these observations confirm earlier reports on the hydrolysis of pressure-treated proteins (Heremans & Heremans, 1989;Ruan et al 1997 ;Iametti et al 1998Iametti et al a, 1999, and provide yet more evidence that the accessibility of cleavage sites in the protein substrate -rather than the intrinsic catalytic ability of a given protease -is what limits the effectiveness of the enzyme action on actual protein substrates.…”

Section: Resultssupporting

confidence: 90%

“…As shown in Fig. 3, pressure treatment alone resulted in a marginal decrease in the immunoreactivity of b-lg, confirming previous observations on b-lg and other proteins (Bonomi et al 1999(Bonomi et al , 2000Iametti et al 1998aIametti et al , 1999. However, a marked decrease in immunoreactivity (no less than ten-fold with respect to the native protein) was observed in the b-lg samples treated under pressure in the presence of chymotrypsin or trypsin.…”

Section: Immunochemical Properties Of the Proteolysis Productssupporting

confidence: 89%

See 1 more Smart Citation

Reduction of immunoreactivity of bovine β-lactoglobulin upon combined physical and proteolytic treatment

Bonomi

Fiocchi

Frøkiær

et al. 2003

Journal of Dairy Research

View full text Add to dashboard Cite

Bovine β-lactoglobulin was hydrolyzed with trypsin or chymotrypsin before, during and after treatment at 600 MPa and pH 6·8 for 10 min at 30, 37 and 44 °C. The extent of β-lactoglobulin hydrolysis under pressure was noticeably higher than at atmospheric pressure, particularly when chymotrypsin was used. Addition of proteases at ambient pressure to previously pressure-treated β-lactoglobulin gave only a modest increase in proteolysis with respect to the untreated protein. Products of enzyme hydrolysis under pressure were separated by reverse-phase HPLC, and were found to be different from those obtained at atmospheric pressure when chymotrypsin was used. The residual immunochemical reactivity of the products of combined pressure-enzyme treatment was assessed on the unresolved hydrolysates by ELISA tests using polyclonal and monoclonal antibodies, and on individual hydrolytic fractions by Western Blotting using sera of paediatric patients allergic to whey proteins in cow milk. The immunoreactivity of the whole hydrolysates was related to their content of residual intact β-lactoglobulin, and no immunochemical reactivity was found for all the products of chymotrypsin hydrolysis under pressure. The results indicate that chymotrypsin effectively hydrolysed hydrophobic regions of β-lactoglobulin that were transiently exposed during the pressure treatments and that were not accessible in the native protein or in the protein that had been previously pressure treated.

show abstract

Section: Resultssupporting

confidence: 90%

Section: Immunochemical Properties Of the Proteolysis Productssupporting

confidence: 89%

Reduction of immunoreactivity of bovine β-lactoglobulin upon combined physical and proteolytic treatment

Bonomi

Fiocchi

Frøkiær

et al. 2003

Journal of Dairy Research

View full text Add to dashboard Cite

show abstract

“…According to the solubility data discussed above, hydrophobic interactions are relevant to the associative behavior of buckwheat proteins and to its modification upon treatment. To assess more specifically the nature of these changes, we used a spectrofluorimetric approach based on the binding of a fluorescent hydrophobic probe (ANS), which has been extensively used to monitor process-induced structural changes in food proteins , , . In this case, we used solid-state spectrofluorimetry to carry out these probe-binding studies, since this approach provides information about the structural changes occurring in the system without resorting to denaturing or dissociating extraction procedures.…”

Section: Resultsmentioning

confidence: 99%

Macromolecular Interactions and Rheological Properties of Buckwheat-Based Dough Obtained from Differently Processed Grains

Mariotti

Lucisano

Pagani

et al. 2008

J. Agric. Food Chem.

Self Cite

View full text Add to dashboard Cite

The physicochemical properties of the protein and starch fractions of flour obtained from buckwheat grains that were previously dehulled or puffed after dehulling were investigated. Dehulling removed most of the nonprotein, nonstarch components of the grain, without affecting the chemical and structural features of the protein and starch components, as made evident by microstructural and spectroscopic measurements. Puffing resulted in extensive modifications of the interprotein network as well as in most of the properties of the buckwheat starch. Flours obtained from dehulled or puffed after dehulling grains were blended with 60-80% wheat flour and tested for their dough-making ability. Blends containing dehulled and puffed buckwheat flours gave dough of much lower quality than dehulled, but had water-holding properties that may be of interest for the shelf life of baked products.

show abstract

“…One of the most valuable and widely used noncovalent hydrophobicity probes is 1-anilino-8-naphthalenesulfonate (ANS). ANS has been used in studies concerning process-induced modification of isolated food proteins − and of complex food systems undergoing processes of various natures − .…”

Section: Introductionmentioning

confidence: 99%

Molecular Basis of the Interaction between Proteins of Plant Origin and Proanthocyanidins in a Model Wine System

Granato

Piano

Nasi

et al. 2010

J. Agric. Food Chem.

View full text Add to dashboard Cite

Plant proteins are being used as a replacement for animal proteins in wine fining. The surface hydrophobicity of plant proteins in four commercial preparations differing for their origin and processing was assessed by using a fluorescent hydrophobic probe in wine-like media. Displacement of the probe by addition of wine phenolics was measured as a way to compare and predict to some extent the efficiency of these proteins in wine fining. It was found that the binding of polyphenols was much more specific than that of the hydrophobic probe. Further analysis of the polyphenol pattern in protein-treated wine-like solutions pointed out two relevant facts: (1) proteins may interfere with the chemistry of the interactions between polyphenols and other wine components; (2) individual protein preparation having different surface hydrophobicities also have different specificities in binding different polymeric forms of the polyphenols and in their substitution products. These findings are related to the possible carry-over of transition metals and may be worth exploring for custom tailoring the fining process. Whether the practical application of the latter finding will call for production and/or screening of plant-derived proteins with features appropriate to this task remains to be investigated. However, the approaches presented in this study may be used for large-scale screening of protein suitability for fining application under laboratory conditions, providing guidelines for their use in actual winemaking applications.

show abstract

Properties of a Soluble Form of High-Pressure-Treated Egg Albumen

Cited by 3 publications

References 4 publications

Reduction of immunoreactivity of bovine β-lactoglobulin upon combined physical and proteolytic treatment

Reduction of immunoreactivity of bovine β-lactoglobulin upon combined physical and proteolytic treatment

Macromolecular Interactions and Rheological Properties of Buckwheat-Based Dough Obtained from Differently Processed Grains

Molecular Basis of the Interaction between Proteins of Plant Origin and Proanthocyanidins in a Model Wine System

Contact Info

Product

Resources

About