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	Provedor de dados Ciênc. Tecnol. Aliment. (1) BJMBR (1) Autor ALVES,Érika de Pádua (1) Bolean,M. (1) Ciancaglini,P. (1) KAKUNO,Amanda Sayuri Senoo (1) Leitão,D.P.S. (1) MORIOKA,Luiz Rodrigo Ito (1) PAIÃO,Fernanda Gonzales (1) Paulino,T.P. (1) SUGUIMOTO,Hélio Hiroshi (1) Spadaro,A.C.C. (1) TAKIHARA,Anderson Massaro (1) Thedei Jr.,G. (1) VIANA,Caroline dos Santos (1) Mais... Palavra-chave Cell permeabilization (2) Enzyme activity (1) Enzyme extraction (1) F-type ATPase (1) Lactose hydrolysis (1) Microbial biotechnology (1) P-type ATPase (1) Streptococcus mutans (1) Toluene permeabilization (1) Mais... Tipo do documento Info:eu-repo/semantics/article (2) Ano 2019 (1) 2008 (1) País Brazil (2) Idioma Inglês (2)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 2 Primeira ... 1 ... Última Toluene permeabilization differentially affects F- and P-type ATPase activities present in the plasma membrane of Streptococcus mutans BJMBR Thedei Jr.,G.; Leitão,D.P.S.; Bolean,M.; Paulino,T.P.; Spadaro,A.C.C.; Ciancaglini,P.. Streptococcus mutans membrane-bound P- and F-type ATPases are responsible for H+ extrusion from the cytoplasm thus keeping intracellular pH appropriate for cell metabolism. Toluene-permeabilized bacterial cells have long been used to study total membrane-bound ATPase activity, and to compare the properties of ATPase in situ with those in membrane-rich fractions. The aim of the present research was to determine if toluene permeabilization can significantly modify the activity of membrane-bound ATPase of both F-type and P-type. ATPase activity was assayed discontinuously by measuring phosphate release from ATP as substrate. Treatment of S. mutans membrane fractions with toluene reduced total ATPase activity by approximately 80% and did not allow... Tipo: Info:eu-repo/semantics/article Palavras-chave: Cell permeabilization; F-type ATPase; P-type ATPase; Toluene permeabilization; Streptococcus mutans. Ano: 2008 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2008001200002 Concentrated beta-galactosidase and cell permeabilization from Saccharomyces fragilis IZ 275 for beta-galactosidase activity in the hydrolysis of lactose Ciênc. Tecnol. Aliment. MORIOKA,Luiz Rodrigo Ito; VIANA,Caroline dos Santos; ALVES,Érika de Pádua; PAIÃO,Fernanda Gonzales; TAKIHARA,Anderson Massaro; KAKUNO,Amanda Sayuri Senoo; SUGUIMOTO,Hélio Hiroshi. Abstract The cheese whey shows an organic nutrient charge that can be used to obtain metabolites of interest by biotechnology of microorganisms. Thus, fermentative processes for enzyme production, in particular beta-galactosidase becomes feasible. The enzyme plays an important role in the biotech food industry to obtain milk and dairy products with low lactose content for consumption by intolerant individuals. The objective of this work was to determine the enzyme activity of the concentrated beta-galactosidase (CBG) and the permeabilized cells (PC) both obtained from Saccharomyces fragilis IZ 275. The enzyme beta-galactosidase obtained from the fermentation of Saccharomyces fragilis IZ 275 in cheese whey was used to determine the optimal conditions for... Tipo: Info:eu-repo/semantics/article Palavras-chave: Enzyme activity; Microbial biotechnology; Cell permeabilization; Lactose hydrolysis; Enzyme extraction. Ano: 2019 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612019000300524 Registros recuperados: 2 Primeira ... 1 ... Última

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