@misc{swaisgood_wang_allen_2001, title={Protein ingredient for carrying lipophilic nutrients}, volume={6,290,974}, number={2001 Sept. 18}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Swaisgood, H. E. and Wang, Q.-W. and Allen, J. C.}, year={2001} }
 @article{wang_allen_swaisgood_1999, title={Binding of lipophilic nutrients to beta-lactoglobulin prepared by bioselective adsorption}, volume={82}, ISSN={["0022-0302"]}, DOI={10.3168/jds.S0022-0302(99)75231-8}, abstractNote={The binding of the lipophilic nutrients, retinal, vitamin D2, and retinyl palmitate by beta-lactoglobulin was measured by analysis of changes in the fluorescence of the tryptophanyl residue of beta-lactoglobulin or the retinyl moiety. The fluorescence intensity of the tryptophanyl residue was quenched by retinoid or vitamin D binding but was enhanced by palmitate binding. The analysis of competitive binding experiments with palmitate indicated that retinal and palmitate did not compete for the same site; however, vitamin D2, which binds with a stoichiometry of 2, appeared to displace palmitate at higher concentrations. Also, the retinoids and vitamin D2 were bound more tightly than was palmitate. The results are consistent with the model in which the retinoids and vitamin D2 bind in the calyx formed by the beta-barrel; palmitate and a second molecule of vitamin D2 bind in a surface pocket near the dimer contact region. Retinyl palmitate, which has both moieties, appeared to bind at both sites.}, number={2}, journal={JOURNAL OF DAIRY SCIENCE}, author={Wang, QW and Allen, JC and Swaisgood, HE}, year={1999}, month={Feb}, pages={257–264} }
 @article{wang_allen_swaisgood_1998, title={Protein concentration dependence of palmitate binding to beta-lactoglobulin}, volume={81}, ISSN={["1525-3198"]}, DOI={10.3168/jds.S0022-0302(98)75553-5}, abstractNote={Abstract The binding of palmitate to β -lactoglobulin at protein concentrations ranging from 1 to 200 μM was determined using an ultrafiltration method with [ 14 C]palmitate. Fit of the data to theoretical models required the assumption of two independent sets of binding sites; however, binding characteristics were dependent on the protein concentration. A model assuming one set of sites on the protein monomer and another on the dimer was consistent with the data. The analysis suggests that 2mol of palmitate are bound/mol of dimer and that the binding constant is of the order of 10 5 M –1 ; a larger number of palmitate molecules are bound per mole of monomer with a smaller binding constant of the order of 10 4 M –1 . Apparently, formation of the dimer, by hydrophobic interactions at the monomer contact site, eliminated palmitate binding sites on the monomer but formed a higher affinity pocket for binding to the dimer.}, number={1}, journal={JOURNAL OF DAIRY SCIENCE}, author={Wang, QWQ and Allen, JC and Swaisgood, HE}, year={1998}, month={Jan}, pages={76–81} }
 @article{wang_allen_swaisgood_1997, title={Binding of retinoids to beta-lactoglobulin isolated by bioselective adsorption}, volume={80}, ISSN={["0022-0302"]}, DOI={10.3168/jds.S0022-0302(97)76029-6}, abstractNote={Abstract Binding of the retinoids, all-trans -retinol, all- trans -retinal, all-trans -retinyl acetate, and all-trans -retinoic acid, to β-lactoglobulin (LG) (96% purity) that had been prepared by bioselective adsorption on N-retinyl-Celite TM was determined from changes in the fluorescence quenching (332nm) of the protein tryptophanyl residues. High affinity binding of all of these compounds occurred at pH 7.0, and the apparent dissociation constant ranged from 1.7 to 3.6 × 10 –8 M . Furthermore, a stoichiometry of 1.0 mol·mol –1 of protein was obtained for each case, indicating that all of the sites in the protein preparation were available. When β-LG in whey protein isolate (57.4% β-LG) was studied, a stoichiometry of 0.65 to 0.82 mol·mol –1 of protein was obtained, indicating that a large number of the sites already had bound lipid or that the protein had been denatured. As the pH was lowered toward 5.15, the affinity decreased about fourfold, but the stoichiometry of binding was unchanged. Far UV circular dichroism spectra indicated that the secondary structure of the protein was not significantly affected by ligand binding; however, the near UV spectra were changed, indicating that the flexibility of tryptophanyl residues decreased. The latter effect is consistent with the change in fluorescence quenching and suggests that a tryptophan is in the binding site.}, number={6}, journal={JOURNAL OF DAIRY SCIENCE}, author={Wang, QW and Allen, JC and Swaisgood, HE}, year={1997}, month={Jun}, pages={1047–1053} }
 @article{wang_allen_swaisgood_1997, title={Binding of vitamin D and cholesterol to beta-lactoglobulin}, volume={80}, ISSN={["0022-0302"]}, DOI={10.3168/jds.S0022-0302(97)76030-2}, abstractNote={Abstract β -Lactoglobulin was isolated directly from acidic whey by bioselective adsorption on N-retinyl-Celite TM , yielding preparations of ≥96% purity. Interactions of these preparations with vitamin D 2 , vitamin D 3 , ergosterol, cholesterol, and 7-dehydrocholesterol were examined by following changes in the fluorescence spectra. Both the excitation and emission spectra indicated that energy was transferred between the tryptophanyl residues of the protein and the chromophore of the ligand. Analyses of the fluorescence changes that occurred upon titration of β -LG with the various ligands allowed determination of the dissociation constant for the complex and the number of moles bound per mole of protein. The affinity for vitamin D 2 (dissociation constant of 4.91 n M ) was 10-fold higher than that of the other compounds, except for ergosterol, which was 5-fold larger than the others. Also, the affinity was 10-fold higher than that typically reported for the retinoids. Furthermore, the value obtained for the number of moles bound per mole of protein was 2 mol·mol –1 for each of the ligands examined in this study; it has been well established that all of the retinoids are bound with a stoichiometry of 1.0. These results suggest that β -LG may be a better carrier of vitamin D than of vitamin A.}, number={6}, journal={JOURNAL OF DAIRY SCIENCE}, author={Wang, QW and Allen, JC and Swaisgood, HE}, year={1997}, month={Jun}, pages={1054–1059} }
 @article{heddleson_allen_wang_swaisgood_1997, title={Purity and yield of beta-lactoglobulin isolated by an N-retinyl-Celite bioaffinity column}, volume={45}, ISSN={["0021-8561"]}, DOI={10.1021/jf9605198}, abstractNote={A bioaffinity column of all-trans-retinal immobilized on Celite was capable of isolating high-purity (94.5%) β-lactoglobulin from bovine acid whey. Conditions for producing a potentially hypoallergenic reduced β-lactoglobulin whey were investigated. Reapplication of pH 5.1 eluate to the column resulted in a final purity of 87% α-lactalbumin. The purity of β-lactoglobulin was slightly lower upon elution with buffers containing <0.4 M sodium phosphate, whereas the yield from desorbing buffers <0.1 M decreased to approximately 40% of that obtained with 0.4 M sodium phosphate. Desorption with low phosphate concentration was improved when pH was increased, suggesting that desorption involves titration of a protophilic group on β-lactoglobulin. These findings suggest that the retinal matrix shows promise in its application for creating hypoallergenic products and the isolation of high-purity β-lactoglobulin with useful functional properties. Keywords: β-Lactoglobulin; α-lactalbumin; bioselective adsorption; N-r...}, number={7}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={Heddleson, RA and Allen, JC and Wang, QW and Swaisgood, HE}, year={1997}, month={Jul}, pages={2369–2373} }