@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 NaCl), 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 of a particulate gel, Texture Profile Analysis (TPA) of the 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={A 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 was twofold larger than that of the intact protein. Examination of the emulsion by scanning electron microscopy revealed that the oil droplets formed with the domain peptides were smaller than those formed with intact protein. Keywords: β-Lactoglobulin; tryptic hydrolysate; limited proteolysis; immobilized trypsin; emulsifying properties; β-barrel domain}, 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={ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTImmobilization of biotinylated transglutaminase by bioselective adsorption to immobilized avidin and characterization of the immobilized activityXiaolin L. Huang, George L. Catignani, and Harold E. SwaisgoodCite this: J. Agric. Food Chem. 1995, 43, 4, 895–901Publication Date (Print):April 1, 1995Publication History Published online1 May 2002Published inissue 1 April 1995https://doi.org/10.1021/jf00052a009RIGHTS & PERMISSIONSArticle Views156Altmetric-Citations15LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit PDF (3 MB) Get e-Alerts Get e-Alerts}, 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={ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTComparison of the Size and Rate of Formation of Peptides Released by Limited Proteolysis of .beta.-Lactoglobulins A and B with Immobilized TrypsinXiaolin L. Huang, George L. Catignani, and Harold E. SwaisgoodCite this: J. Agric. Food Chem. 1994, 42, 6, 1281–1284Publication Date (Print):June 1, 1994Publication History Published online1 May 2002Published inissue 1 June 1994https://doi.org/10.1021/jf00042a005RIGHTS & PERMISSIONSArticle Views88Altmetric-Citations13LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit PDF (1 MB) Get e-Alerts Get e-Alerts}, 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={ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTRelative Structural Stabilities of .beta.-Lactoglobulins A and B as Determined by Proteolytic Susceptibility and Differential Scanning CalorimetryXiaolin L. Huang, George L. Catignani, and Harold E. SwaisgoodCite this: J. Agric. Food Chem. 1994, 42, 6, 1276–1280Publication Date (Print):June 1, 1994Publication History Published online1 May 2002Published inissue 1 June 1994https://doi.org/10.1021/jf00042a004RIGHTS & PERMISSIONSArticle Views123Altmetric-Citations29LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit PDF (2 MB) Get e-Alerts Get e-Alerts}, 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} }