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THERMOSTABILITY OF ANTIOXIDANT AND DETERIORATIVE ENZYMES FROM SOURSOP AND CASHEW APPLE JUICES Rev. Bras. Frutic.
RABELO,MARCELA CRISTINA; BRITO,EDY SOUSA DE; MOURA,CARLOS FARLEY HERBSTER; OLIVEIRA,LUCIANA DE SIQUEIRA; MIRANDA,MARIA RAQUEL ALCÂNTARA DE.
ABSTRACT This work aimed to evaluate the thermostability of antioxidant (superoxide dismutase - SOD, catalase - CAT and ascorbate peroxidase - APX) and deteriorative (guaiacol peroxidase - G-POD, polyphenoloxidase - PPO, pectin-methylesterase - PME and polygalacturonase - PG) enzymes from soursop and cashew apple juices. Juices were prepared homogenizing ripe fruit pulps and submitting to different thermal treatments (55, 65, 75, 85 and 95°C) for different time period (1, 3, 5, 10, 15, 20 and 30 min) then enzymatic activities were evaluated. The treatments at 55°C for soursop juice and at 75°C for cashew apple juice presented the best results, considering the low residual activities for deteriorative enzymes and the retained activity of SOD. Our results...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Pasteurization; Enzyme kinetics; Thermal inactivation; Annona muricata; Anacardium occidentale.
Ano: 2016 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-29452016000200801
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Purification and characterization of cytosolic and cell wall β-galactosidases from Vigna unguiculata stems Braz. J. Plant Physiol.
Sudério,Fabrício Bonfim; Barbosa,Gislainy Karla da Costa; Gomes-Filho,Enéas; Enéas-Filho,Joaquim.
Three β-galactosidase isoforms, β-gal I and β-gal II (cytosolic) and β-gal III (cell wall-associated), were isolated from stems of Vigna unguiculata (L.) Walp. cv. Pitiúba seedlings. Purification consisted of aμMonia sulfate fractionation followed by chromatography in DEAE-Sephadex and Lactosyl-Sepharose columns. The two cytosolic isoforms showed the same chromatography pattern, which differed from that of β-gal III. Electrophoresis revealed a single band of protein for β-gal II and β-gal III which also expressed β-galactosidase activity in gel. The apparent molecular mass of the β-gal I, II and III was 89, 146 and 124 kDa, respectively. The three isoforms revealed the same optimal pH (4.0) and the same optimal assay temperature (55ºC) for enzyme activity....
Tipo: Info:eu-repo/semantics/article Palavras-chave: Enzymatic kinetics; Cowpea; Optimal pH; Enzyme purification; Thermal stability; Thermal inactivation.
Ano: 2011 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1677-04202011000100003
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Pectin methylesterase activity determined by different methods and thermal inactivation of exogenous pme in mango juice Ciência e Agrotecnologia
Gonzalez,Samantha Lemke; Lima,Regina Cristina Aparecida; Carneiro,Eliana Beleski Borba; Almeida,Mareci Mendes de; Rosso,Neiva Deliberali.
Pectin methylesterase (PME) hydrolyzes methyl ester groups in pectin chains to form carboxylic groups, releasing methanol and H3O+. The aim of this study was to determine PME activity in samples of pectinases by UV-VIS spectroscopy, to measure the acid and methanol produced in the reaction of pectin with pectinase and to verify the thermal inactivation of exogenous PME in mango juice. The activity of PME in samples of pectinase was determined by potentiometry, UV-VIS spectroscopy, and by the action of alcohol oxidase. The reaction showed greater activity at pH 4.0 to 4.5 and at a temperature of 45° C. PME activity determined by UV-VIS spectroscopy with bromophenol blue indicator showed a good correlation with the activity determined by potentiometry and...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Pectin metilesterase; Activity; Thermal inactivation; Mango juice.
Ano: 2011 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1413-70542011000500017
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