dc.creatorMacedo, JA
dc.creatorCavallieri, ALF
dc.creatorda Cunha, RL
dc.creatorSato, HH
dc.date2010
dc.dateOCT
dc.date2014-11-15T01:42:55Z
dc.date2015-11-26T17:35:46Z
dc.date2014-11-15T01:42:55Z
dc.date2015-11-26T17:35:46Z
dc.date.accessioned2018-03-29T00:17:53Z
dc.date.available2018-03-29T00:17:53Z
dc.identifierInternational Dairy Journal. Elsevier Sci Ltd, v. 20, n. 10, n. 673, n. 679, 2010.
dc.identifier0958-6946
dc.identifierWOS:000281518200003
dc.identifier10.1016/j.idairyj.2010.03.014
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/73775
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/73775
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/73775
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1285646
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionThe influence of the transglutaminase (TG) from a newly isolated Brazilian Streptomyces sp. CBMAI 837 and sodium caseinate concentration (4% and 8%, w/w) on acid-gel properties was studied. Standard gels with and without commercial transglutaminase samples were tested in parallel. The mechanical properties of the samples (stress and strain at rupture and elasticity modulus) were evaluated using uniaxial compression measurements. Texture parameters showed that the commercial TG gels had greater values of elasticity modulus, while addition of the Streptomyces sp. CBMAI 837 TG to the gel led to the formation of less elastic, but more deformable gels. The electrophoresis results showed that the commercial TG enzyme in this system promoted higher molecular mass protein polymers than the enzyme from Streptomyces sp. CBMAI 837. Microscopy and water-holding capacity (WHC) observations showed that all the gel characteristics could be associated with specific interactions promoted by each TG tested. (C) 2010 Elsevier Ltd. All rights reserved.
dc.description20
dc.description10
dc.description673
dc.description679
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.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.languageen
dc.publisherElsevier Sci Ltd
dc.publisherOxford
dc.publisherInglaterra
dc.relationInternational Dairy Journal
dc.relationInt. Dairy J.
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectGlucono-delta-lactone
dc.subjectMicrobial Transglutaminase
dc.subjectCross-linking
dc.subjectPurification
dc.subjectGels
dc.subjectSyneresis
dc.subjectProteins
dc.subjectSucrose
dc.subjectEnzyme
dc.subjectStrain
dc.titleThe effect of transglutaminase from Streptomyces sp CBMAI 837 on the gelation of acidified sodium caseinate
dc.typeArtículos de revistas


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