dc.creatorTribst, AAL
dc.creatorCristianini, M
dc.date2012
dc.dateOCT
dc.date2014-07-30T16:51:39Z
dc.date2015-11-26T16:33:37Z
dc.date2014-07-30T16:51:39Z
dc.date2015-11-26T16:33:37Z
dc.date.accessioned2018-03-28T23:15:33Z
dc.date.available2018-03-28T23:15:33Z
dc.identifierInnovative Food Science & Emerging Technologies. Elsevier Sci Ltd, v. 16, n. 355, n. 360, 2012.
dc.identifier1466-8564
dc.identifierWOS:000314193000046
dc.identifier10.1016/j.ifset.2012.08.002
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/62681
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/62681
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1270921
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionHigh pressure homogenization (HPH) has been described as a process able to change enzyme activity and stability of enzymes. This study investigated the HPH effects on commercial glucose oxidase (GO) activity. Enzyme solutions at pH 5.0, 5.7 and 6.5 were processed at pressures 50, 100, and 150 MPa. The HPH effects were determined by the enzyme residual activity measured at 15, 50 and 75 degrees C immediately after homogenization and after 1 day of storage. Results showed that low pressures (50 MPa) reduced the GO relative activity at all temperatures evaluated when samples were homogenized at pH 5.0. However, a relative recovery of enzyme activity was observed when homogenization was carried out at pressures of >= 100 MPa. For samples processed at pH 5.7, the homogenization at 100 MPa reduced the relative enzyme activity at 15 and 50 degrees C. On the contrary, a 25% improvement on GO relative activity at 75 degrees C was observed after homogenization at 150 MPa. For samples homogenized at pH 6.5, the process continuously reduced the GO relative activity at 15 degrees C and almost no changes were observed when activity was evaluated at 50 and 75 degrees C. After 1 day, the GO relative activity of homogenized samples could increase up to 400%, as compared to the native one stored under the same condition. The results confirmed that HPH changes the GO activity, being able to increase or decrease it. This activity change may be associated to continuous modifications in enzyme structure due to homogenization pressure and pH of solution. Additionally, the GO relative stability increase in aqueous solution highlights HPH as an interesting tool to improve GO performance, expanding the potential application range of glucose oxidase in food industry. Industrial relevance: GO is an important enzyme in food industry due to its ability to consume oxygen and glucose. However its high instability on food matrix limits GO application. Therefore, the application of high pressure homogenization as an emerging technology to keep enzyme activity in aqueous solution is interesting to improve GO applications. (C) 2012 Elsevier Ltd. All rights reserved.
dc.description16
dc.description355
dc.description360
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFAPESP [2010/02540-1]
dc.languageen
dc.publisherElsevier Sci Ltd
dc.publisherOxford
dc.publisherInglaterra
dc.relationInnovative Food Science & Emerging Technologies
dc.relationInnov. Food Sci. Emerg. Technol.
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectGlucose oxidase
dc.subjectUltra-high pressure homogenization
dc.subjectNon-thermal process
dc.subjectEnzyme activity
dc.subjectDynamic High-pressure
dc.subjectOrange Juice
dc.subjectAspergillus-niger
dc.subjectPectin Methylesterase
dc.subjectMango Nectar
dc.subjectInactivation
dc.subjectQuality
dc.titleChanges in commercial glucose oxidase activity by high pressure homogenization
dc.typeArtículos de revistas


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