@article{wilcox_clare_valentine_swaisgood_2002, title={Immobilization and utilization of the recombinant fusion proteins trypsin-streptavidin and streptavidin-transglutaminase for modification of whey protein isolate functionality}, volume={50}, ISSN={["1520-5118"]}, DOI={10.1021/jf011603c}, abstractNote={A method was developed for the production of a hydrolyzed/polymerized whey protein derivative with altered solution and gelation properties using a combination of recombinant DNA and immobilized enzyme technologies. The recombinant fusion proteins trypsin-streptavidin (TrypSA) and streptavidin-transglutaminase (cSAcTG) were produced in Escherichia coli, extracted, and then immobilized by selective adsorption on biotinylated controlled-pore glass. Recirculation through a TrypSA reactor induced limited proteolysis of whey proteins. Hydrolysates were then recirculated through a cSAcTG reactor for incremental periods of time to arrive at increasing degrees of polymerization. The polymers were subsequently analyzed for viscosity/flow behavior, gelation properties, and fracture properties using shear rate ramps/intrinsic viscosity, small-strain oscillatory rheology, and vane viscometry, respectively. By combining limited proteolysis with controlled cross-linking, it was possible to create derivatives of whey proteins with enhanced functional properties. Increases in the degree of whey protein modification were correlated with greater apparent viscosity and intrinsic viscosity, lowered gel point temperatures, and stronger, more brittle gels. This method allowed for recycling of the enzyme, eliminated the requirement for a downstream inactivation step, and permitted control over the extent of modification. Utilization of a similar process may allow for the production of designer proteins engineered with specific functionalities.}, number={13}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={Wilcox, CP and Clare, DA and Valentine, VW and Swaisgood, HE}, year={2002}, month={Jun}, pages={3723–3730} }
 @article{wilcox_janolino_swaisgood_2002, title={Isolation and partial characterization of CD36 from skim milk}, volume={85}, ISSN={["0022-0302"]}, DOI={10.3168/jds.S0022-0302(02)74265-3}, abstractNote={CD36, a common milk fat globule membrane glycoprotein, was isolated from skim milk by methods similar to those previously utilized for the isolation of sulfhydryl oxidase. Two separate methods that were employed, gave similar purity as observed by electrophoresis. The first was based on differential centrifugation and size-exclusion chromatography, whereas the second combined ultrafiltration and affinity chromatography. After significant purification, the protein was identified by Western blotting and sequence analysis. Deglycosylation decreased the apparent molecular mass from approximately 85 to 57 kDa. These results suggested tissue-specific glycosylation. The purified fractions also exhibited low levels of sulfhydryl oxidase activity, the significance of which will require further study.}, number={8}, journal={JOURNAL OF DAIRY SCIENCE}, author={Wilcox, CP and Janolino, VG and Swaisgood, HE}, year={2002}, month={Aug}, pages={1903–1908} }
 @article{wilcox_swaisgood_2002, title={Modification of the rheological properties of whey protein isolate through the use of an immobilized microbial transglutaminase}, volume={50}, ISSN={["1520-5118"]}, DOI={10.1021/jf0117154}, abstractNote={A process was developed in which calcium-independent, microbial transglutaminase (mTgase) was immobilized to controlled-pore glass. Avidin was adsorbed to glass beads that had been derivatized and biotinylated. The enzyme was biotinylated and adsorbed to the avidin affinity matrix. Solutions of 8% whey protein isolate (WPI) were then incubated with the mTgase beads, resulting in limited cross-linking of whey proteins. As incubation time increased, intrinsic viscosity increased, gelation temperature decreased, and stronger, more brittle gels were formed upon heating. This process allowed for recycling of the enzyme, eliminated the requirement for a downstream inactivation step, and permitted control over the extent of cross-linking. The functional properties of several batches of WPI were modified using <10 mg of the same enzyme, illustrating the capacity of immobilized enzymes to be used more frequently in applications of this nature.}, number={20}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={Wilcox, CP and Swaisgood, HE}, year={2002}, month={Sep}, pages={5546–5551} }
 @article{wilcox_weissinger_long_fitzmaurice_mirkov_swaisgood_1997, title={Production and purification of an active bovine lysozyme in tobacco (Nicotiana tabacum): Utilization of value-added crop plants traditionally grown under intensive agriculture}, volume={45}, ISSN={["0021-8561"]}, DOI={10.1021/jf970156r}, abstractNote={The goals of this study were to express bovine lysozyme in tobacco and to purify the protein with a scaleable process to >90% homogeneity while retaining antimicrobial characteristics. Results showed that the enzyme was expressed at levels equivalent to 1−1.5% of total fraction 2 protein in each of five different transformant groups. The enzyme was subsequently purified to 93% homogeneity using an easily scaleable process while retaining high activity. It was concluded that tobacco was an excellent choice for expression of the recombinant protein and that the purification process developed in this study demonstrates methodology for isolation of high-value enzymes from tobacco and other crop plants. Keywords: Transgenic; lysozyme; recombinant protein; antimicrobial; Nicotiana tabacum}, number={7}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={Wilcox, CP and Weissinger, AK and Long, RC and Fitzmaurice, LC and Mirkov, TE and Swaisgood, HE}, year={1997}, month={Jul}, pages={2793–2797} }
 @inproceedings{grattapaglia_chaparro_wilcox_mccord_crane_amerson_werner_liu_o'malley_whetten_et al._1993, title={Application of genetic markers to tree breeding}, booktitle={Proceedings of the 22nd Southern Forest Tree Improvement Conference}, author={Grattapaglia, D. and Chaparro, J. and Wilcox, P. and McCord, S. and Crane, B. and Amerson, H. and Werner, D. and Liu, B. H. and O'Malley, D. and Whetten, R. and et al.}, year={1993}, pages={452–463} }