dc.creator | Sabadin, Isabele Serimarco | |
dc.creator | Villas-Boas, Mariana Battaglin | |
dc.creator | Zollner, Ricardo de Lima | |
dc.creator | Netto, Flavia Maria | |
dc.date | 2012 | |
dc.date | 2013-09-19T18:06:36Z | |
dc.date | 2016-06-30T18:49:35Z | |
dc.date | 2013-09-19T18:06:36Z | |
dc.date | 2016-06-30T18:49:35Z | |
dc.date.accessioned | 2018-03-29T01:53:02Z | |
dc.date.available | 2018-03-29T01:53:02Z | |
dc.identifier | European Food Research and Technology. Springer, v.235, n.5, p.801-809, 2012 | |
dc.identifier | 1438-2377 | |
dc.identifier | WOS:000309869500005 | |
dc.identifier | 10.1007/s00217-012-1802-z | |
dc.identifier | http://www.repositorio.unicamp.br/jspui/handle/REPOSIP/2298 | |
dc.identifier | http://repositorio.unicamp.br/jspui/handle/REPOSIP/2298 | |
dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/1308304 | |
dc.description | Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) | |
dc.description | The effect of combined treatments of hydrolysis with different proteases, and subsequent polymerization with transglutaminase on the antigenic activity of beta-Lg was studied. For the hydrolysis of beta-Lg using Alcalase, Neutrase or bromelain, the reaction conditions were 3 % beta-Lg and enzyme:substrate 25 U g(-1) of protein, as was defined using factorial study. Under these conditions, the degree of hydrolysis (DH) of the hydrolysates was 12.6 % when obtained with Alcalase and approximately 4 % with Neutrase or bromelain. Post-hydrolysis polymerization did not result in an increase in molecular mass of the protein, but these samples presented a lower DH, determined by trinitrobenzenosulfonic acid (TNBS) method, suggesting that polymerization had occurred. Hydrolysis with the three enzymes reduced the beta-Lg antigenicity, as evaluated by ELISA and immunoblotting analyses. The IgE-binding responses were practically null (< 9 mu g mL(-1)), 22.82 and 55.73 mu g mL(-1) towards the hydrolysates obtained with Alcalase, bromelain, and Neutrase, respectively. The post-hydrolysis polymerization increased or had no significant effect (P a parts per thousand yen 0.05) on the antigenic response of the hydrolysates. | |
dc.description | 235 | |
dc.description | 5 | |
dc.description | 801 | |
dc.description | 809 | |
dc.description | Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) | |
dc.description | Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) | |
dc.language | eng | |
dc.publisher | Springer | |
dc.publisher | New York | |
dc.relation | European Food Research and Technology | |
dc.rights | fechado | |
dc.source | WOS | |
dc.subject | Hydrolysis | |
dc.subject | Crosslink | |
dc.subject | Transglutaminase | |
dc.subject | Antigenicity | |
dc.subject | Bovine milk proteins | |
dc.subject | ENZYMATIC CROSS-LINKING | |
dc.subject | COWS MILK ALLERGY | |
dc.subject | WHEY PROTEINS | |
dc.subject | MICROBIAL TRANSGLUTAMINASE | |
dc.subject | HIGH-PRESSURE | |
dc.subject | ALPHA-LACTALBUMIN | |
dc.subject | CELL EPITOPES | |
dc.subject | IGE-BINDING | |
dc.subject | ALLERGENICITY | |
dc.subject | ACID | |
dc.title | Effect of combined treatment of hydrolysis and polymerization with transglutaminase on beta-lactoglobulin antigenicity | |
dc.type | Artículos de revistas | |