[ { "key": "49X5U5AC", "version": 1, "library": { "type": "user", "id": 19532, "name": "Antonio Guadix", "links": { "alternate": { "href": "https://www.zotero.org/antonioguadix", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/users/19532/items/49X5U5AC", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/antonioguadix/items/49X5U5AC", "type": "text/html" }, "up": { "href": "https://api.zotero.org/users/19532/items/3Q74T7HF", "type": "application/json" } }, "meta": {}, "data": { "key": "49X5U5AC", "version": 1, "parentItem": "3Q74T7HF", "itemType": "attachment", "linkMode": "imported_url", "title": "Scopus - Journal of Chromatography A: Hydrophilic interaction chromatography coupled to electrospray mass spectrometry for the separation of peptides and protein digests", "accessDate": "2009-10-07T11:54:02Z", "url": "http://www.scopus.com/record/display.url?eid=2-s2.0-67249106337&view=basic&origin=inward&txGid=fZK2eaqvM2a4QGDYUHGBv0w%3a39", "note": "", "contentType": "text/html", "charset": "utf-8", "filename": "display.html", "md5": null, "mtime": 1254916446000, "tags": [], "relations": {}, "dateAdded": "2009-10-07T11:54:02Z", "dateModified": "2009-10-07T11:54:02Z" } }, { "key": "3Q74T7HF", "version": 1, "library": { "type": "user", "id": 19532, "name": "Antonio Guadix", "links": { "alternate": { "href": "https://www.zotero.org/antonioguadix", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/users/19532/items/3Q74T7HF", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/antonioguadix/items/3Q74T7HF", "type": "text/html" } }, "meta": { "creatorSummary": "Yang et al.", "parsedDate": "2009", "numChildren": 1 }, "data": { "key": "3Q74T7HF", "version": 1, "itemType": "journalArticle", "title": "Hydrophilic interaction chromatography coupled to electrospray mass spectrometry for the separation of peptides and protein digests", "creators": [ { "creatorType": "author", "firstName": "Y.", "lastName": "Yang" }, { "creatorType": "author", "firstName": "R.I.", "lastName": "Boysen" }, { "creatorType": "author", "firstName": "M.T.W.", "lastName": "Hearn" } ], "abstractNote": "In this study, the analysis of a peptide set, chosen for their differences in hydrophilicity, and the tryptic digests of bovine cytochrome c and β-lactoglobulin by hydrophilic interaction chromatography-electrospray ionisation mass spectrometry (HILIC-ESI-MS) is demonstrated. Two different types of HILIC phases, i.e., an amide- and an amino-modified silica-based phase, packed into narrow bore or capillary columns, were investigated with separations conducted under either low pH or neutral pH conditions. The separation performance of the two HILIC columns with respect to peak efficiency and selectivity have been documented under these different mobile phase conditions, and the results compared with the performance of a conventional capillary reversed-phase C18 column of similar dimensions. It was found that very good separation of the peptide set could be achieved by using the amide-modified silica column over a broad pH range. Moreover, with the protein digest samples, excellent separation of the tryptic digests was obtained with the amide-modified HILIC column under neutral pH conditions. Compared to the conventional reversed-phase C18 separations, the use of these HILIC columns not only provided complementary separation selectivity, but also offered the capability to identify unique peptides using tandem HILIC-mass spectrometric techniques. These studies therefore highlight the potential of HILIC procedures for future proteomic applications. © 2009 Elsevier B.V. All rights reserved.", "publicationTitle": "Journal of Chromatography A", "publisher": "", "place": "", "date": "2009", "volume": "1216", "issue": "29", "section": "", "partNumber": "", "partTitle": "", "pages": "5518-5524", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "", "citationKey": "", "url": "http://www.scopus.com/inward/record.url?eid=2-s2.0-67249106337&partnerID=40", "accessDate": "2009-10-07T11:53:58Z", "PMID": "", "PMCID": "", "ISSN": "", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "Scopus", "callNumber": "", "rights": "", "extra": "", "tags": [ { "tag": "ESI-MS", "type": 1 }, { "tag": "HILIC", "type": 1 }, { "tag": "Mobile phase pH", "type": 1 }, { "tag": "Peak efficiency", "type": 1 }, { "tag": "Peptides", "type": 1 }, { "tag": "Protein identification", "type": 1 }, { "tag": "Selectivity", "type": 1 } ], "collections": [], "relations": {}, "dateAdded": "2009-10-07T11:53:58Z", "dateModified": "2009-10-07T11:53:58Z" } }, { "key": "D6G7S2KZ", "version": 1, "library": { "type": "user", "id": 19532, "name": "Antonio Guadix", "links": { "alternate": { "href": "https://www.zotero.org/antonioguadix", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/users/19532/items/D6G7S2KZ", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/antonioguadix/items/D6G7S2KZ", "type": "text/html" }, "up": { "href": "https://api.zotero.org/users/19532/items/I8F568KI", "type": "application/json" } }, "meta": {}, "data": { "key": "D6G7S2KZ", "version": 1, "parentItem": "I8F568KI", "itemType": "attachment", "linkMode": "imported_url", "title": "ScienceDirect Snapshot", "accessDate": "2009-10-07T11:52:12Z", "url": "http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6TG8-4X1J74J-2&_user=654849&_rdoc=1&_fmt=&_orig=search&_sort=d&_docanchor=&view=c&_acct=C000035398&_version=1&_urlVersion=0&_userid=654849&md5=4818ee52a0246e89f13faf461040ccb9", "note": "", "contentType": "text/html", "charset": "utf-8", "filename": "science.html", "md5": null, "mtime": 1254916332000, "tags": [], "relations": {}, "dateAdded": "2009-10-07T11:52:12Z", "dateModified": "2009-10-07T11:52:12Z" } }, { "key": "5FFC39JW", "version": 1, "library": { "type": "user", "id": 19532, "name": "Antonio Guadix", "links": { "alternate": { "href": "https://www.zotero.org/antonioguadix", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/users/19532/items/5FFC39JW", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/antonioguadix/items/5FFC39JW", "type": "text/html" }, "up": { "href": "https://api.zotero.org/users/19532/items/I8F568KI", "type": "application/json" } }, "meta": { "numChildren": false }, "data": { "key": "5FFC39JW", "version": 1, "parentItem": "I8F568KI", "itemType": "attachment", "linkMode": "imported_url", "title": "ScienceDirect Full Text PDF", "accessDate": "2009-10-07T11:52:10Z", "url": "http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6TG8-4X1J74J-2-K&_cdi=5248&_user=654849&_orig=search&_coverDate=10%2F02%2F2009&_sk=987839959&view=c&wchp=dGLzVzz-zSkWz&md5=cd1e9876cbb5cfa7655b41eb2ef26e57&ie=/sdarticle.pdf", "note": "", "contentType": "application/pdf", "charset": "", "filename": "Krenkova et al. - 2009 - High binding capacity surface grafted monolithic c.pdf", "md5": "c11dcbcb3aa59ef97058efe439d6beee", "mtime": 1254916330000, "tags": [], "relations": {}, "dateAdded": "2009-10-07T11:52:10Z", "dateModified": "2009-10-07T11:52:11Z" } }, { "key": "I8F568KI", "version": 1, "library": { "type": "user", "id": 19532, "name": "Antonio Guadix", "links": { "alternate": { "href": "https://www.zotero.org/antonioguadix", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/users/19532/items/I8F568KI", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/antonioguadix/items/I8F568KI", "type": "text/html" } }, "meta": { "creatorSummary": "Krenkova et al.", "parsedDate": "2009-10-02", "numChildren": 2 }, "data": { "key": "I8F568KI", "version": 1, "itemType": "journalArticle", "title": "High binding capacity surface grafted monolithic columns for cation exchange chromatography of proteins and peptides", "creators": [ { "creatorType": "author", "firstName": "Jana", "lastName": "Krenkova" }, { "creatorType": "author", "firstName": "Andrea", "lastName": "Gargano" }, { "creatorType": "author", "firstName": "Nathan A.", "lastName": "Lacher" }, { "creatorType": "author", "firstName": "Jeffrey M.", "lastName": "Schneiderheinze" }, { "creatorType": "author", "firstName": "Frantisek", "lastName": "Svec" } ], "abstractNote": "Poly(glycidyl methacrylate-co-ethylene methacrylate) monoliths have been prepared in 100 [mu]m i.d. capillaries and their epoxy groups hydrolyzed to obtain poly(2,3-dihydroxypropyl methacrylate-co-ethylene methacrylate) matrix. These polymers were then photografted in a single step with 2-acrylamido-2-methyl-1-propanesulfonic acid and acrylic acid to afford stationary phases for a strong and a weak cation exchange chromatography, respectively. Alternatively, poly(ethylene glycol) methacrylate was used for grafting in the first step in order to enhance hydrophilicity of the support followed by photografting with 2-acrylamido-2-methyl-1-propanesulfonic acid or acrylic acid in the second step. These new columns were used for the separation of proteins and peptides. A mixture of ovalbumin, [alpha]-chymotrypsinogen, cytochrome c, ribonuclease A and lysozyme was used to assess the chromatographic performance for large molecules while a cytochrome c digest served as a model mixture of peptides. All tested columns featured excellent mass transfer as demonstrated with very steep breakthrough curves. The highest binding capacities were found for columns prepared using the two step functionalization. Columns with sulfonic acid functionalities adsorbed up to 21.5 mg/mL lysozyme while the capacity of the weak cation exchange column functionalized with acrylic acid was 29.2 mg/mL.", "publicationTitle": "Journal of Chromatography A", "publisher": "", "place": "", "date": "Octubre 2, 2009", "volume": "1216", "issue": "40", "section": "", "partNumber": "", "partTitle": "", "pages": "6824-6830", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "10.1016/j.chroma.2009.08.031", "citationKey": "", "url": "http://www.sciencedirect.com/science/article/B6TG8-4X1J74J-2/2/6920a1a6df442cd39d6fca0a18a87a88", "accessDate": "2009-10-07T11:52:08Z", "PMID": "", "PMCID": "", "ISSN": "0021-9673", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "ScienceDirect", "callNumber": "", "rights": "", "extra": "", "tags": [ { "tag": "Capillary column", "type": 1 }, { "tag": "Glycidyl methacrylate", "type": 1 }, { "tag": "Grafting", "type": 1 }, { "tag": "Ion exchange chromatography", "type": 1 }, { "tag": "Monolith", "type": 1 }, { "tag": "Peptides", "type": 1 }, { "tag": "Proteins", "type": 1 } ], "collections": [], "relations": {}, "dateAdded": "2009-10-07T11:52:08Z", "dateModified": "2009-10-07T11:52:08Z" } }, { "key": "HWS3ZW57", "version": 1, "library": { "type": "user", "id": 19532, "name": "Antonio Guadix", "links": { "alternate": { "href": "https://www.zotero.org/antonioguadix", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/users/19532/items/HWS3ZW57", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/antonioguadix/items/HWS3ZW57", "type": "text/html" }, "up": { "href": "https://api.zotero.org/users/19532/items/JZX95TJP", "type": "application/json" } }, "meta": {}, "data": { "key": "HWS3ZW57", "version": 1, "parentItem": "JZX95TJP", "itemType": "attachment", "linkMode": "imported_url", "title": "ScienceDirect Snapshot", "accessDate": "2009-10-07T11:48:42Z", "url": "http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6VP9-4W1BVB0-1&_user=654849&_coverDate=12%2F31%2F2009&_rdoc=13&_fmt=high&_orig=browse&_srch=doc-info(%23toc%236201%232009%23999769991%231494136%23FLA%23display%23Volume)&_cdi=6201&_sort=d&_docanchor=&_ct=62&_acct=C000035398&_version=1&_urlVersion=0&_userid=654849&md5=ba82b42d7e10cf890aa8fb6e13eb1e0a", "note": "", "contentType": "text/html", "charset": "utf-8", "filename": "science.html", "md5": null, "mtime": 1254916122000, "tags": [], "relations": {}, "dateAdded": "2009-10-07T11:48:42Z", "dateModified": "2009-10-07T11:48:42Z" } }, { "key": "JFZWZ3S8", "version": 1, "library": { "type": "user", "id": 19532, "name": "Antonio Guadix", "links": { "alternate": { "href": "https://www.zotero.org/antonioguadix", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/users/19532/items/JFZWZ3S8", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/antonioguadix/items/JFZWZ3S8", "type": "text/html" }, "up": { "href": "https://api.zotero.org/users/19532/items/JZX95TJP", "type": "application/json" } }, "meta": { "numChildren": false }, "data": { "key": "JFZWZ3S8", "version": 1, "parentItem": "JZX95TJP", "itemType": "attachment", "linkMode": "imported_url", "title": "ScienceDirect Full Text PDF", "accessDate": "2009-10-07T11:48:40Z", "url": "http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6VP9-4W1BVB0-1-1&_cdi=6201&_user=654849&_orig=browse&_coverDate=12%2F31%2F2009&_sk=999769991&view=c&wchp=dGLzVlz-zSkzV&md5=145f3e1b43e2670159361e58c12a3a48&ie=/sdarticle.pdf", "note": "", "contentType": "application/pdf", "charset": "", "filename": "Souza et al. - 2009 - Effect of moderate electric fields in the permeati.pdf", "md5": "8a0681f670010cdf68fd436b36282860", "mtime": 1254916120000, "tags": [], "relations": {}, "dateAdded": "2009-10-07T11:48:40Z", "dateModified": "2009-10-07T11:48:41Z" } }, { "key": "JZX95TJP", "version": 1, "library": { "type": "user", "id": 19532, "name": "Antonio Guadix", "links": { "alternate": { "href": "https://www.zotero.org/antonioguadix", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/users/19532/items/JZX95TJP", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/antonioguadix/items/JZX95TJP", "type": "text/html" } }, "meta": { "creatorSummary": "Souza et al.", "parsedDate": "2009-12", "numChildren": 2 }, "data": { "key": "JZX95TJP", "version": 1, "itemType": "journalArticle", "title": "Effect of moderate electric fields in the permeation properties of chitosan coatings", "creators": [ { "creatorType": "author", "firstName": "B.W.S.", "lastName": "Souza" }, { "creatorType": "author", "firstName": "M.A.", "lastName": "Cerqueira" }, { "creatorType": "author", "firstName": "A.", "lastName": "Casariego" }, { "creatorType": "author", "firstName": "A.M.P.", "lastName": "Lima" }, { "creatorType": "author", "firstName": "J.A.", "lastName": "Teixeira" }, { "creatorType": "author", "firstName": "A.A.", "lastName": "Vicente" } ], "abstractNote": "Edible films and coatings can provide additional protection for food, while being a fully biodegradable, environmentally friendly packaging system. Preliminary works have shown that the presence of a moderate electric field during the preparation of chitosan coating solutions may influence e.g. their transport properties. If such effect is confirmed, moderate electric fields could be used to tailor edible films and coatings for specific applications. The aim of this work was to determine the effect of field strength on functional properties of chitosan coatings (obtained from lobster from the Cuban coasts). Four different field strengths were tested (50, 100, 150, 200 V cm-1) and, for each electric field treatment, the water vapor, oxygen and carbon dioxide permeabilities of the films formed were determined, together with their color, opacity and solubility in water. The surface microstructure of the films was analyzed using atomic force microscopy (AFM).\nThe results showed that ohmic heating had statistically significant effects on film's physical properties and structure. In general, the most pronounced effect of the field strength was observed for treatments made at 100 V cm-1 or higher, a positive correlation being found between the water vapor, oxygen and carbon dioxide permeability coefficients and field strength. The AFM results show that the surface of chitosan films is much more uniform when an electric field is applied, which may be related with a more uniform gel structure leading to the differences observed in terms of transport properties.", "publicationTitle": "Food Hydrocolloids", "publisher": "", "place": "", "date": "Diciembre 2009", "volume": "23", "issue": "8", "section": "", "partNumber": "", "partTitle": "", "pages": "2110-2115", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "10.1016/j.foodhyd.2009.03.021", "citationKey": "", "url": "http://www.sciencedirect.com/science/article/B6VP9-4W1BVB0-1/2/e3edfc94905be8c59e559746f1f2db8a", "accessDate": "2009-10-07T11:48:38Z", "PMID": "", "PMCID": "", "ISSN": "0268-005X", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "ScienceDirect", "callNumber": "", "rights": "", "extra": "", "tags": [ { "tag": "Chitosan films", "type": 1 }, { "tag": "Edible coatings", "type": 1 }, { "tag": "Edible films", "type": 1 }, { "tag": "Moderate electric fields", "type": 1 } ], "collections": [], "relations": {}, "dateAdded": "2009-10-07T11:48:38Z", "dateModified": "2009-10-07T11:48:38Z" } }, { "key": "FXK6XPP5", "version": 1, "library": { "type": "user", "id": 19532, "name": "Antonio Guadix", "links": { "alternate": { "href": "https://www.zotero.org/antonioguadix", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/users/19532/items/FXK6XPP5", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/antonioguadix/items/FXK6XPP5", "type": "text/html" }, "up": { "href": "https://api.zotero.org/users/19532/items/7BDTSF4T", "type": "application/json" } }, "meta": { "numChildren": false }, "data": { "key": "FXK6XPP5", "version": 1, "parentItem": "7BDTSF4T", "itemType": "attachment", "linkMode": "imported_url", "title": "Wiley Interscience PDF", "accessDate": "2009-10-07T11:46:28Z", "url": "http://www3.interscience.wiley.com/cgi-bin/fulltext?ID=121686124&PLACEBO=IE.pdf&mode=pdf", "note": "", "contentType": "application/pdf", "charset": "", "filename": "Schmidt et al. - 2009 - Size exclusion chromatography coupled to electrosp.pdf", "md5": "7ba5cc678090baffd8c82b309d166377", "mtime": 1254915990000, "tags": [], "relations": {}, "dateAdded": "2009-10-07T11:46:28Z", "dateModified": "2009-10-07T11:46:29Z" } }, { "key": "7BDTSF4T", "version": 1, "library": { "type": "user", "id": 19532, "name": "Antonio Guadix", "links": { "alternate": { "href": "https://www.zotero.org/antonioguadix", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/users/19532/items/7BDTSF4T", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/antonioguadix/items/7BDTSF4T", "type": "text/html" } }, "meta": { "creatorSummary": "Schmidt et al.", "parsedDate": "2009", "numChildren": 1 }, "data": { "key": "7BDTSF4T", "version": 1, "itemType": "journalArticle", "title": "Size exclusion chromatography coupled to electrospray ionization mass spectrometry for analysis and quantitative characterization of arsenic interactions with peptides and proteins", "creators": [ { "creatorType": "author", "firstName": "Anne-Christine", "lastName": "Schmidt" }, { "creatorType": "author", "firstName": "Benjamin", "lastName": "Fahlbusch" }, { "creatorType": "author", "firstName": "Matthias", "lastName": "Otto" } ], "abstractNote": "Arsenic-binding proteins are of toxicological importance since enzymatic activities can be blocked by arsenic interactions. In the present work, a novel methodology based on size exclusion chromatography coupled to electrospray ionization mass spectrometry (SEC-ESI-MS) was developed with special emphasis to preserve the intact proteins and their arsenic bindings. The eluent composition of 25 mMTris/HCl, pH 7.5, with the addition of 100-mM NaCl optimized for SEC with UV detection provided the highest SEC separation efficiency, but was not compatible with the ESI-MS because of the non-volatility of the buffer substance and of the salt additive. In order to find the best compromise between chromatographic separation and ionization of the arsenic-binding proteins, buffer type and concentration, pH value, portion of organic solvent in the SEC eluent as well as the flow rate were varied. In the optimized procedure five different arsenic-binding peptides and proteins (glutathione, oxytocin, aprotinin, alpha-lactalbumin, thioredoxin) covering a molar mass range of 0.3-14 kDa could be analyzed using 75% 10-mM ammonium formate, pH 5.0/25% acetonitrile (v : v) as eluent and a turbo ion spray source operated at 300 °C and 5.5 kV. A complete differentiation of all peptides and proteins involved in the arsenic-binding studies as well as of their arsenic-bound forms has become feasible by means of the extracted ion chromatograms (XIC) of the mass spectrometric detection. The new method offered the possibility to estimate equilibrium constants for the reaction of phenylarsine oxide with different thiol-containing biomolecules by means of the XIC peak areas of reactants and products. Limits of detection in the range of 2-10 µM were obtained by SEC-ESI-MS for the individual proteins. Copyright © 2009 John Wiley & Sons, Ltd.", "publicationTitle": "Journal of Mass Spectrometry", "publisher": "", "place": "", "date": "2009", "volume": "44", "issue": "6", "section": "", "partNumber": "", "partTitle": "", "pages": "898-910", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "10.1002/jms.1563", "citationKey": "", "url": "http://dx.doi.org/10.1002/jms.1563", "accessDate": "2009-10-07T11:46:27Z", "PMID": "", "PMCID": "", "ISSN": "", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "Wiley InterScience", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [], "relations": {}, "dateAdded": "2009-10-07T11:46:27Z", "dateModified": "2009-10-07T11:46:27Z" } }, { "key": "TKIQ79PP", "version": 1, "library": { "type": "user", "id": 19532, "name": "Antonio Guadix", "links": { "alternate": { "href": "https://www.zotero.org/antonioguadix", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/users/19532/items/TKIQ79PP", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/antonioguadix/items/TKIQ79PP", "type": "text/html" }, "up": { "href": "https://api.zotero.org/users/19532/items/J25HNXB5", "type": "application/json" } }, "meta": {}, "data": { "key": "TKIQ79PP", "version": 1, "parentItem": "J25HNXB5", "itemType": "attachment", "linkMode": "imported_url", "title": "ScienceDirect Snapshot", "accessDate": "2009-10-07T11:42:19Z", "url": "http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6VP9-4W9XDY4-1&_user=654849&_coverDate=12%2F31%2F2009&_rdoc=21&_fmt=high&_orig=browse&_srch=doc-info(%23toc%236201%232009%23999769991%231494136%23FLA%23display%23Volume)&_cdi=6201&_sort=d&_docanchor=&_ct=62&_acct=C000035398&_version=1&_urlVersion=0&_userid=654849&md5=5a916a7e0485729e3314c0e4ffe648f1", "note": "", "contentType": "text/html", "charset": "utf-8", "filename": "science.html", "md5": null, "mtime": 1254915742000, "tags": [], "relations": {}, "dateAdded": "2009-10-07T11:42:19Z", "dateModified": "2009-10-07T11:42:19Z" } }, { "key": "5ATWMHIT", "version": 1, "library": { "type": "user", "id": 19532, "name": "Antonio Guadix", "links": { "alternate": { "href": "https://www.zotero.org/antonioguadix", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/users/19532/items/5ATWMHIT", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/antonioguadix/items/5ATWMHIT", "type": "text/html" }, "up": { "href": "https://api.zotero.org/users/19532/items/J25HNXB5", "type": "application/json" } }, "meta": { "numChildren": false }, "data": { "key": "5ATWMHIT", "version": 1, "parentItem": "J25HNXB5", "itemType": "attachment", "linkMode": "imported_url", "title": "ScienceDirect Full Text PDF", "accessDate": "2009-10-07T11:42:14Z", "url": "http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6VP9-4W9XDY4-1-1&_cdi=6201&_user=654849&_orig=browse&_coverDate=12%2F31%2F2009&_sk=999769991&view=c&wchp=dGLbVlb-zSkWA&md5=bbaba7324f773c4bb20fed9b8059e3aa&ie=/sdarticle.pdf", "note": "", "contentType": "application/pdf", "charset": "", "filename": "Kuropatwa et al. - 2009 - Impact of pH on the interactions between whey and .pdf", "md5": "09f17a86ff1ddcafb591295d5bacd2e4", "mtime": 1254915740000, "tags": [], "relations": {}, "dateAdded": "2009-10-07T11:42:14Z", "dateModified": "2009-10-07T11:42:18Z" } }, { "key": "8G25BQWW", "version": 1, "library": { "type": "user", "id": 19532, "name": "Antonio Guadix", "links": { "alternate": { "href": "https://www.zotero.org/antonioguadix", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/users/19532/items/8G25BQWW", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/antonioguadix/items/8G25BQWW", "type": "text/html" }, "up": { "href": "https://api.zotero.org/users/19532/items/55Z78VUV", "type": "application/json" } }, "meta": { "numChildren": false }, "data": { "key": "8G25BQWW", "version": 1, "parentItem": "55Z78VUV", "itemType": "attachment", "linkMode": "imported_url", "title": "ScienceDirect Full Text PDF", "accessDate": "2009-10-07T11:42:05Z", "url": "http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6VP9-4W6Y11J-1-1&_cdi=6201&_user=654849&_orig=browse&_coverDate=12%2F31%2F2009&_sk=999769991&view=c&wchp=dGLbVzW-zSkzV&md5=3f13c45113153c1dfd59e2375fd6fda0&ie=/sdarticle.pdf", "note": "", "contentType": "application/pdf", "charset": "", "filename": "Day et al. - 2009 - Interfacial properties of deamidated wheat protein.pdf", "md5": "05994db78701feec10b1b502f9384d9b", "mtime": 1254915738000, "tags": [], "relations": {}, "dateAdded": "2009-10-07T11:42:05Z", "dateModified": "2009-10-07T11:42:16Z" } }, { "key": "J25HNXB5", "version": 1, "library": { "type": "user", "id": 19532, "name": "Antonio Guadix", "links": { "alternate": { "href": "https://www.zotero.org/antonioguadix", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/users/19532/items/J25HNXB5", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/antonioguadix/items/J25HNXB5", "type": "text/html" } }, "meta": { "creatorSummary": "Kuropatwa et al.", "parsedDate": "2009-12", "numChildren": 2 }, "data": { "key": "J25HNXB5", "version": 1, "itemType": "journalArticle", "title": "Impact of pH on the interactions between whey and egg white proteins as assessed by the foamability of their mixtures", "creators": [ { "creatorType": "author", "firstName": "Malgorzata", "lastName": "Kuropatwa" }, { "creatorType": "author", "firstName": "Alexander", "lastName": "Tolkach" }, { "creatorType": "author", "firstName": "Ulrich", "lastName": "Kulozik" } ], "abstractNote": "The impact of protein-protein interactions on foaming properties of mixtures consisting of egg white proteins (EWP) and whey proteins (WP) with total protein content of 60 g/L was examined at pH 5, 7 and 9. The ratio between EWP and WP in the mixtures was varied between 67:33, 50:50 and 33:67 (in %; w/w). The ionic strength was adjusted to that of milk (I = 176 mM). The foamability of the protein products was characterized by the foam capacity, stability and firmness. In addition, the hydrophobicity in the protein solutions was assessed as a measure for the physical behaviour and ability of proteins to adsorb at the air-water interface.\nThe individual egg white proteins and whey proteins each showed the best foaming properties at pH 5 and pH 9, respectively. At pH 9 a synergism was observed in the capacity and stability of the foams from EWP/WP-mixtures. This effect appears to be caused by the electrostatic interactions between egg white and whey proteins which occur in the bulk solution after the pH adjustment prior to the foaming. In contrast, at pH 5 no positive influence of foaming the components in a mixture as well as no indication of intermolecular interactions was found. At pH value near the pI of ovalbumin the protein interactions occur when the proteins have adsorbed at the air-water interface. The protein systems foamed at pH 7 showed intermediate foamability compared to the values obtained at alkaline and acidic pH.", "publicationTitle": "Food Hydrocolloids", "publisher": "", "place": "", "date": "Diciembre 2009", "volume": "23", "issue": "8", "section": "", "partNumber": "", "partTitle": "", "pages": "2174-2181", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "10.1016/j.foodhyd.2009.05.001", "citationKey": "", "url": "http://www.sciencedirect.com/science/article/B6VP9-4W9XDY4-1/2/73ab8c9e2b8b129456f41d949252c849", "accessDate": "2009-10-07T11:42:11Z", "PMID": "", "PMCID": "", "ISSN": "0268-005X", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "ScienceDirect", "callNumber": "", "rights": "", "extra": "", "tags": [ { "tag": "Egg white", "type": 1 }, { "tag": "Foaming properties", "type": 1 }, { "tag": "Hydrophobicity of the solution", "type": 1 }, { "tag": "Protein interactions", "type": 1 }, { "tag": "Whey protein", "type": 1 } ], "collections": [], "relations": {}, "dateAdded": "2009-10-07T11:42:11Z", "dateModified": "2009-10-07T11:42:11Z" } }, { "key": "ZX2D2K2E", "version": 1, "library": { "type": "user", "id": 19532, "name": "Antonio Guadix", "links": { "alternate": { "href": "https://www.zotero.org/antonioguadix", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/users/19532/items/ZX2D2K2E", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/antonioguadix/items/ZX2D2K2E", "type": "text/html" }, "up": { "href": "https://api.zotero.org/users/19532/items/55Z78VUV", "type": "application/json" } }, "meta": {}, "data": { "key": "ZX2D2K2E", "version": 1, "parentItem": "55Z78VUV", "itemType": "attachment", "linkMode": "imported_url", "title": "ScienceDirect Snapshot", "accessDate": "2009-10-07T11:42:06Z", "url": "http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6VP9-4W6Y11J-1&_user=654849&_coverDate=12%2F31%2F2009&_rdoc=19&_fmt=high&_orig=browse&_srch=doc-info(%23toc%236201%232009%23999769991%231494136%23FLA%23display%23Volume)&_cdi=6201&_sort=d&_docanchor=&_ct=62&_acct=C000035398&_version=1&_urlVersion=0&_userid=654849&md5=5896a39d8f20feb85b0302d5397a5aa9", "note": "", "contentType": "text/html", "charset": "utf-8", "filename": "science.html", "md5": null, "mtime": 1254915728000, "tags": [], "relations": {}, "dateAdded": "2009-10-07T11:42:06Z", "dateModified": "2009-10-07T11:42:06Z" } }, { "key": "55Z78VUV", "version": 1, "library": { "type": "user", "id": 19532, "name": "Antonio Guadix", "links": { "alternate": { "href": "https://www.zotero.org/antonioguadix", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/users/19532/items/55Z78VUV", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/antonioguadix/items/55Z78VUV", "type": "text/html" } }, "meta": { "creatorSummary": "Day et al.", "parsedDate": "2009-12", "numChildren": 2 }, "data": { "key": "55Z78VUV", "version": 1, "itemType": "journalArticle", "title": "Interfacial properties of deamidated wheat protein in relation to its ability to stabilise oil-in-water emulsions", "creators": [ { "creatorType": "author", "firstName": "Li", "lastName": "Day" }, { "creatorType": "author", "firstName": "Mi", "lastName": "Xu" }, { "creatorType": "author", "firstName": "Leif", "lastName": "Lundin" }, { "creatorType": "author", "firstName": "Tim J.", "lastName": "Wooster" } ], "abstractNote": "Isolated wheat protein (IWP) is an acidic deamidated wheat protein. The deamidation process enhances the protein solubility at pHs greater than 6, and therefore its potential ability to act as a food emulsifier. The interfacial properties and the mechanism by which this protein stabilises oil-in-water emulsions were investigated by measuring the protein's absorbed layer thickness on latex particles, its interfacial rheology, and the colloidal and thermal stability of IWP stabilised emulsions. IWP forms a relatively thick interfacial layer of 18 nm upon adsorption onto latex beads, suggesting that the protein adsorbed with the long axis perpendicular to the surface, i.e. end-on, at a full protein coverage. The interfacial rheology measurement showed that IWP formed a relatively weak fluid-like interface. Similar to other protein emulsifiers, the colloidal stability of IWP emulsions is provided largely through electrostatic repulsion. Although IWP emulsions were sensitive to salt induced flocculation, the presence of excess protein in the aqueous phase (e.g. 4 wt%) was able to reduce the effect of salt screening (50 mM CaCl2) on a 25 wt% oil-in-water emulsion completely. The emulsions underwent minimal coalescence when droplets were in close contact, e.g. flocculated, because the interfacial layer of IWP provides a barrier to droplet coalescence, even in high salt environments. IWP emulsions were resistant to thermal treatment with no changes in particle size observed when the emulsions were heated (up to 90 °C for 20 min) in the absence or the presence of 150 mM NaCl. The heat stability of IWP emulsions is thought to arise from the structure of IWP at the interface. A lack of free cysteines combined with few hydrophobic regions meant that there were minimal interactions between protein molecules adsorbed onto the same droplet or on neighbouring droplets. The unique interfacial properties of IWP, e.g. its physical layer thickness and the structure provide enhanced stability for emulsions against coalescence and heating.", "publicationTitle": "Food Hydrocolloids", "publisher": "", "place": "", "date": "Diciembre 2009", "volume": "23", "issue": "8", "section": "", "partNumber": "", "partTitle": "", "pages": "2158-2167", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "10.1016/j.foodhyd.2009.04.004", "citationKey": "", "url": "http://www.sciencedirect.com/science/article/B6VP9-4W6Y11J-1/2/5e5a7b541225c5d6779334c6685dca91", "accessDate": "2009-10-07T11:42:03Z", "PMID": "", "PMCID": "", "ISSN": "0268-005X", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "ScienceDirect", "callNumber": "", "rights": "", "extra": "", "tags": [ { "tag": "Deamidated wheat protein", "type": 1 }, { "tag": "Emulsion colloidal stability", "type": 1 }, { "tag": "Emulsion thermal stability", "type": 1 }, { "tag": "Interfacial layer thickness", "type": 1 }, { "tag": "Protein surface architecture", "type": 1 } ], "collections": [], "relations": {}, "dateAdded": "2009-10-07T11:42:03Z", "dateModified": "2009-10-07T11:42:03Z" } }, { "key": "VJXPDSDI", "version": 1, "library": { "type": "user", "id": 19532, "name": "Antonio Guadix", "links": { "alternate": { "href": "https://www.zotero.org/antonioguadix", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/users/19532/items/VJXPDSDI", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/antonioguadix/items/VJXPDSDI", "type": "text/html" }, "up": { "href": "https://api.zotero.org/users/19532/items/D7CXVIV7", "type": "application/json" } }, "meta": {}, "data": { "key": "VJXPDSDI", "version": 1, "parentItem": "D7CXVIV7", "itemType": "attachment", "linkMode": "imported_url", "title": "ScienceDirect Snapshot", "accessDate": "2009-07-21T22:11:26Z", "url": "http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6TFX-4V476YK-G&_user=10&_coverDate=01%2F15%2F2009&_rdoc=14&_fmt=high&_orig=browse&_srch=doc-info(%23toc%235238%232009%23997649998%23757178%23FLP%23display%23Volume)&_cdi=5238&_sort=d&_docanchor=&_ct=29&_acct=C000050221&_version=1&_urlVersion=0&_userid=10&md5=36101f592fe28fab06f39c4f6eddcc1e", "note": "", "contentType": "text/html", "charset": "utf-8", "filename": "science.html", "md5": null, "mtime": null, "tags": [], "relations": {}, "dateAdded": "2009-07-21T22:11:26Z", "dateModified": "2009-07-21T22:11:26Z" } }, { "key": "D7CXVIV7", "version": 1, "library": { "type": "user", "id": 19532, "name": "Antonio Guadix", "links": { "alternate": { "href": "https://www.zotero.org/antonioguadix", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/users/19532/items/D7CXVIV7", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/antonioguadix/items/D7CXVIV7", "type": "text/html" } }, "meta": { "creatorSummary": "Wang et al.", "parsedDate": "2009-01", "numChildren": 1 }, "data": { "key": "D7CXVIV7", "version": 1, "itemType": "journalArticle", "title": "A comparative study of removal of Cu(II) from aqueous solutions by locally low-cost materials: marine macroalgae and agricultural by-products", "creators": [ { "creatorType": "author", "firstName": "Xue Song", "lastName": "Wang" }, { "creatorType": "author", "firstName": "Zhi Zhong", "lastName": "Li" }, { "creatorType": "author", "firstName": "Cheng", "lastName": "Sun" } ], "abstractNote": "aDepartment of Chemical Engineering, Huaihai Institute of Technology, Lianyungang, Jiangsu, 222005, China bSchool of the Environment, Nanjing University, Nanjing, Jiangsu 210093, China In this study, adsorption of Cu(II) onto the five locally abundantly low-cost biosorbents (Laminaria japonica, P. yezoensis Ueda, rice bran, wheat bran and walnut hull) was investigated depending on initial solution pH, contact time, adsorbent concentration and reaction temperature. Cu(II) removal was pH-dependent for various biosorbents investigated. For P. yezoensis Ueda, rice bran, wheat bran and walnut hull, the batch equilibrium data were correlated to Langmuir and Freundlich isotherms and the data fitted better to the Langmuir isotherm equation and yielded Langmuir monolayer capacity of 5.04, 10.41, 6.85 and 3.52 mg/g at the temperature of 20°C, respectively. In the case of Laminaria japonica, the equilibrium data obeyed the Hill-der Boer equation for the whole initial concentration ranges of 0–200 mg/L examined, but only to Langmuir and Freundlich equations for the initial concentration less than 120 mg/L at various temperatures. The apparent thermodynamic parameters were calculated for each of the five biosorbents (ΔH = 9.25–40.04 kJ/mol; ΔG = –17.60 to –24.16 kJ/mol and ΔS = 85.81–228 J/mol K). The numerical values obtained showed that Cu(II) adsorption is a spontaneous, entropy-driven and endothermic process. The batch kinetic data were correlated to the pseudo-first order and pseudo-second order models and the data fitted better to the pseudo-second order equation (the pseudo-second order rate constants, k2,e = 0.1059–0.9453 g/(mg min); the correlation coefficients, r = 0.9816–0.9993). Keywords: Biosorption; Cu(II); Marine algae; Agricultural by-products; Hill-der Boer equation", "publicationTitle": "Desalination", "publisher": "", "place": "", "date": "January 2009", "volume": "235", "issue": "1-3", "section": "", "partNumber": "", "partTitle": "", "pages": "146-159", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "10.1016/j.desal.2008.02.008", "citationKey": "", "url": "http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6TFX-4V476YK-G&_user=10&_coverDate=01%2F15%2F2009&_rdoc=14&_fmt=high&_orig=browse&_srch=doc-info(%23toc%235238%232009%23997649998%23757178%23FLP%23display%23Volume)&_cdi=5238&_sort=d&_docanchor=&_ct=29&_acct=C000050221&_version=1&_urlVersion=0&_userid=10&md5=36101f592fe28fab06f39c4f6eddcc1e", "accessDate": "2009-07-21T22:11:24Z", "PMID": "", "PMCID": "", "ISSN": "", "archive": "", "archiveLocation": "", "shortTitle": "A comparative study of removal of Cu(II) from aqueous solutions by locally low-cost materials", "language": "", "libraryCatalog": "ScienceDirect", "callNumber": "", "rights": "", "extra": "", "tags": [ { "tag": "Agricultural by-products", "type": 1 }, { "tag": "Biosorption", "type": 1 }, { "tag": "Cu(II)", "type": 1 }, { "tag": "Hill-der Boer equation", "type": 1 }, { "tag": "Marine algae", "type": 1 } ], "collections": [], "relations": {}, "dateAdded": "2009-07-21T22:11:24Z", "dateModified": "2009-07-21T22:11:24Z" } }, { "key": "TM24UI7W", "version": 1, "library": { "type": "user", "id": 19532, "name": "Antonio Guadix", "links": { "alternate": { "href": "https://www.zotero.org/antonioguadix", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/users/19532/items/TM24UI7W", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/antonioguadix/items/TM24UI7W", "type": "text/html" }, "up": { "href": "https://api.zotero.org/users/19532/items/IB5DG4H8", "type": "application/json" } }, "meta": {}, "data": { "key": "TM24UI7W", "version": 1, "parentItem": "IB5DG4H8", "itemType": "attachment", "linkMode": "imported_url", "title": "ScienceDirect Snapshot", "accessDate": "2009-07-21T22:11:20Z", "url": "http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6TFX-4V476YK-8&_user=10&_coverDate=01%2F15%2F2009&_rdoc=8&_fmt=high&_orig=browse&_srch=doc-info(%23toc%235238%232009%23997649998%23757178%23FLP%23display%23Volume)&_cdi=5238&_sort=d&_docanchor=&_ct=29&_acct=C000050221&_version=1&_urlVersion=0&_userid=10&md5=8b8d3fadb6485685f374997c227799ae", "note": "", "contentType": "text/html", "charset": "utf-8", "filename": "science.html", "md5": null, "mtime": null, "tags": [], "relations": {}, "dateAdded": "2009-07-21T22:11:20Z", "dateModified": "2009-07-21T22:11:20Z" } }, { "key": "IB5DG4H8", "version": 1, "library": { "type": "user", "id": 19532, "name": "Antonio Guadix", "links": { "alternate": { "href": "https://www.zotero.org/antonioguadix", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/users/19532/items/IB5DG4H8", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/antonioguadix/items/IB5DG4H8", "type": "text/html" } }, "meta": { "creatorSummary": "Srinivasan et al.", "parsedDate": "2009-01", "numChildren": 1 }, "data": { "key": "IB5DG4H8", "version": 1, "itemType": "journalArticle", "title": "Decolourisation of leather dye by ozonation", "creators": [ { "creatorType": "author", "firstName": "S.V.", "lastName": "Srinivasan" }, { "creatorType": "author", "firstName": "T.", "lastName": "Rema" }, { "creatorType": "author", "firstName": "K.", "lastName": "Chitra" }, { "creatorType": "author", "firstName": "K. Sri", "lastName": "Balakameswari" }, { "creatorType": "author", "firstName": "R.", "lastName": "Suthanthararajan" }, { "creatorType": "author", "firstName": "B. Uma", "lastName": "Maheswari" }, { "creatorType": "author", "firstName": "E.", "lastName": "Ravindranath" }, { "creatorType": "author", "firstName": "S.", "lastName": "Rajamani" } ], "abstractNote": "aDepartment of Environmental Technology, Central Leather Research Institute, Chennai – 600020, India Sewage and industrial effluent treatment plants are installed with primary and secondary biological treatment units to reduce the discharge of pollution load into the environment. These treatment plants normally reduce the organic load in terms of BOD but not the pollution load in terms of inorganic salts (total dissolved solids—TDS) and colour in the effluent. To eliminate the contamination of ground and surface water bodies and to conserve water sources, the regulatory authorities have taken very stringent regulations to implement zero liquid discharge (ZLD) for industrial effluents, i.e., water recovery from wastewater and reuse. It is difficult to recover water from secondary treated wastewater directly, as it does not meet the reverse osmosis feed requirements. In order to achieve the feed requirements, different tertiary treatment methods are being tried. In this study, removal of colour due to residual dyes has been attempted using ozone. The main purpose of this study is to decolourise the dye used in leather processing. Also, the effect of pH and dye concentration on dye decolourisation has been investigated. From the study it has been observed that maximum decolourisation efficiency up to 97% could be achieved for the pH values (4,7, 9 and 11) and dye concentrations (30, 65, 180 and 360 mg/L) studied. 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