@article{huang_sherk_2014, title={Evaluation and comparison of sustainability performance and visual preference of residential landscape elements}, volume={24}, number={3}, journal={HortTechnology}, author={Huang, X. L. and Sherk, J. T.}, year={2014}, pages={318–324} }
 @article{huang_catignani_swaisgood_1999, title={Modification of rheological properties of whey protein isolates by limited proteolysis}, volume={43}, ISSN={["0027-769X"]}, DOI={10.1002/(SICI)1521-3803(19990301)43:2<79::AID-FOOD79>3.0.CO;2-8}, abstractNote={Whey protein isolate (WPI) was subjected to limited tryptic hydrolysis and the effect of the limited hydrolysis on the rheological properties of WPI was examined and compared with those of untreated WPI. At 10% concentration (w/v in 50 mM TES buffer, pH 7.0, containing 50 mM NaCI), both WPI and the enzyme-treated WPI (EWPI) formed heat-induced viscoelastic gels. However, EWPI formed weaker gels (lower storage modulus) than WPI gels. Moreover, a lower gelation point (77 °C) was obtained for EWPI as compared with that of WPI which gelled at 80 °C only after holding 1.4 min. Thermal analysis and aggregation studies indicated that limited proteolysis resulted in changes in the denaturation and aggregation properties. As a consequenece, EWPI formed particulated gels, while WPI formed fine-stranded gels. In keeping with the formation ofa particulate gel, Texture Profile Analysis (TPA) ofthe heat-induced gels (at 80 °C for 30 min) revealed that EWPI gels possessed significantly higher (p < 0.05) cohesiveness, hardness, gumminess, and chewiness but did not fracture at 75% deformation. The results suggest that the domain peptides, especially β-lactoglobulin domains released by the limited proteolysis, were responsible for the altered gelation properties.}, number={2}, journal={NAHRUNG-FOOD}, author={Huang, XL and Catignani, GL and Swaisgood, HE}, year={1999}, month={Apr}, pages={79–85} }
 @article{huang_catignani_swaisgood_1997, title={Comparison of the properties of trypsin immobilized on 2 Celite(TM) derivatives}, volume={53}, ISSN={["0168-1656"]}, DOI={10.1016/S0168-1656(96)01656-2}, abstractNote={Trypsin was immobilized on 2 Celite derivatives and the kinetic properties of trypsin immobilized on these derivatives were determined and compared. Celite was derivatized with organosilane to give aminopropyl-Celite (APC) and a portion of this derivative was then succinylated to give succinamidopropyl-Celite (SAPC). Trypsin was covalently immobilized on APC using glutaraldehyde to activate amino groups and on SAPC using water-soluble carbodiimide to activate surface carboxyl groups. Enzyme loadings were 13.9 and 17.8 mg ml-1 of beads on APC and SAPC, respectively. Using p-tosyl-L-arginine methyl ester as substrate, the catalyst specific activity, KMapp and kcat/KMapp were 17.8 U ml-1 of beads, 3.60 and 21.0 mM-1 min-1, respectively, for trypsin-APC as compared with 24.5 U ml-1 of beads, 3.77 and 20.3 mM-1 min-1, respectively, for trypsin-SAPC. With beta-lactoglobulin as substrate, KMapp and kcat/KMapp were 0.36 and 1.62 mM-1 min-1 for trypsin-APC and 0.54 and 1.39 mM-1 min-1 for trypsin-SAPC, respectively. The pH range for optimal activity was much larger for both immobilized forms as compared with the soluble enzyme. The optimal temperature ranges were 40-50 degrees C for trypsin-APC and 50-60 degrees C for trypsin-SAPC. The two methods of immobilization on Celite gave biocataysts with similar kinetic properties but immobilization on SAPC yielded slightly higher loadings and higher specific activities.}, number={1}, journal={JOURNAL OF BIOTECHNOLOGY}, author={Huang, XL and Catignani, GL and Swaisgood, HE}, year={1997}, month={Feb}, pages={21–27} }
 @article{huang_catignani_swaisgood_1997, title={Micro-scale method for determining foaming properties of protein}, volume={62}, ISSN={["0022-1147"]}, DOI={10.1111/j.1365-2621.1997.tb15030.x}, abstractNote={ABSTRACTA 5% protein suspension (4 mL) was whipped in a modified 50‐mL centrifuge tube using a tissumizer equipped with a flat‐bottom generator. Drainage time at 50% liquid weight and the weight of the foam formed/unit volume were used for calculating foam stability and foam overrun, respectively. The foaming properties of a variety of milk proteins were determined using this method. This method distinguished differences in foaming properties among the proteins. Values for overrun confirmed published results. Compared with standard methods, this method required much less sample (about 1/20) and less measuring time (about 1/5 to 1/10).}, number={5}, journal={JOURNAL OF FOOD SCIENCE}, author={Huang, XL and Catignani, GL and Swaisgood, HE}, year={1997}, pages={1028-&} }
 @article{huang_catignani_swaisgood_1996, title={Improved emulsifying properties of beta-barrel domain peptides obtained by membrane-fractionation of a limited tryptic hydrolysate of beta-lactoglobulin}, volume={44}, ISSN={["1520-5118"]}, DOI={10.1021/jf960038o}, abstractNote={Fragments of the β-barrel domain of β-lactoglobulin were obtained by membrane fractionation of a limited proteolysate prepared with an immobilized trypsin bioreactor. Analysis of this fraction by size-exclusion chromatography under physiological conditions indicated that the fraction contained a predominant peptide (50%) with a size of 8400 Da and several other peptides with sizes ranging from 2000 to 30 700 Da. Analysis of reductively denatured peptides by sodium dodecyl sulfate polyacrylamide gel electrophoresis in the presence of 2-mercaptoethanol indicated the presence of a major peptide with a size of 6400 Da, suggesting that a small peptide was linked to the 8400-Da peptide by a disulfide bond. Comparison of the surface and emulsifying properties of the peptide fraction with those of intact β-lactoglobulin indicated that the domain peptides have a lower surface hydrophobicity and a slightly higher surface and interfacial tension. Furthermore, the emulsifying activity index for the domain peptides wa...}, number={11}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={Huang, XLL and Catignani, GL and Swaisgood, HE}, year={1996}, month={Nov}, pages={3437–3443} }
 @article{huang_catignani_swaisgood_1995, title={IMMOBILIZATION OF BIOTINYLATED TRANSGLUTAMINASE BY BIOSELECTIVE ADSORPTION TO IMMOBILIZED AVIDIN AND CHARACTERIZATION OF THE IMMOBILIZED ACTIVITY}, volume={43}, ISSN={["0021-8561"]}, DOI={10.1021/jf00052a009}, abstractNote={Transglutaminase was iminobilized on a porous glass support by biotinylation followed by adsorption to avidin that had been immobilized by adsorption to the biotinylated aminopropyl glass. Thus, avidin served as a protein spacer between the support and the enzyme. Both the biotinylation of enzyme amino groups and the association of the biotinylated enzyme with soluble avidin caused some loss of enzyme activity. This loss could account for the 3-fold reduction in the specific activity of the immobilized enzyme with carbobenzoxyglutaminylglycine and hydroxylamine as substrates. However, with α s -casein as a substrate, a 24-fold reduction in the k cat value was observed, implying that the rate of reaction with this large substrate molecule was limited by mass transfer. The pH optima and temperature dependences of enzyme catalysis were similar for both the soluble and immobilized enzyme, although the slight differences observed for the immobilized form were also indicative of mass transfer effects. A bimodal pH activity profile with optima at pH 6.5 and 7.5 was obtained with both enzyme forms. Treatment of α s -casein with immobilized enzyme caused a rapid disappearance of the monomeric protein with concomitant appearance of dimers and higher cross-linked polymers}, number={4}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={HUANG, XL and CATIGNANI, GL and SWAISGOOD, HE}, year={1995}, month={Apr}, pages={895–901} }
 @article{huang_catignani_swaisgood_1994, title={COMPARISON OF THE SIZE AND RATE OF FORMATION OF PEPTIDES RELEASED BY LIMITED PROTEOLYSIS OF BETA-LACTOGLOBULIN-A AND BETA-LACTOGLOBULIN-B WITH IMMOBILIZED TRYPSIN}, volume={42}, ISSN={["1520-5118"]}, DOI={10.1021/jf00042a005}, abstractNote={Proteolytic susceptibility of β-lactoglobulin (β-Lg) genetic variants A and B was determined by subjection to immobilized trypsin. Products of limited proteolysis, performed in 50 mM Tris-HCl buffer (pH 8.0) at 4 o C, were characterized by fractionation with anion-exchange chromatography and by denaturing gel electrophoresis of the isolated fractions. Both the rate of appearance of products and the peptides formed were different for the two variants. Two major peptides, with estimated molecular weights of 7500 and 8200 were obtained in homogeneous form by ion-exchange fractionation of β-Lg A hydrolysates. Similar fractionation of β-Lg B hydrolysates yielded fractions that were heterogeneous, containing larger peptides that were not present in β-Lg A hydrolysates}, number={6}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={HUANG, XL and CATIGNANI, GL and SWAISGOOD, HE}, year={1994}, month={Jun}, pages={1281–1284} }
 @article{huang_catignani_swaisgood_1994, title={RELATIVE STRUCTURAL STABILITIES OF BETA-LACTOGLOBULIN-A AND BETA-LACTOGLOBULIN-B AS DETERMINED BY PROTEOLYTIC SUSCEPTIBILITY AND DIFFERENTIAL SCANNING CALORIMETRY}, volume={42}, ISSN={["1520-5118"]}, DOI={10.1021/jf00042a004}, abstractNote={β-Lactoglobulin (β-Lg) genetic variants A and B were purified from milks of individual cows that were homozygous for each variant, and their structural stabilities were examined by susceptibility to proteolysis by immobilized trypsin and by differential scanning calorimetry (DSC). A 15% increase in the value for V M /K M was observed with proteolysis of β-Lg A as compared with β-Lg B. This observation is substantiated by a more rapid disappearance of intact β-Lg A during proteolysis of equimolar mixtures of the two variants. Lower structural stability of variant A is also indicated by a 5 o C lower thermal denaturation temperature observed for β-Lg A by DSC}, number={6}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={HUANG, XL and CATIGNANI, GL and SWAISGOOD, HE}, year={1994}, month={Jun}, pages={1276–1280} }