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Biochemical characterisation of a glucoamylase from Aspergillus niger produced by solid-state fermentation BABT
Slivinski,Christiane Trevisan; Machado,Alex Vinicius Lopes; Iulek,Jorge; Ayub,Ricardo Antônio; Almeida,Mareci Mendes de.
In this work, glucoamylase was produced by Aspergillus niger in solid-state fermentation. The enzyme was partially purified by ammonium sulphate precipitation and ion exchange and gel filtration chromatographies. Its molecular mass was estimated as 118.17 kDa by electrophoresis. The partially purified enzyme had an optimum pH range of 4.5-5.0 and an optimum temperature of 60 °C, with average activity 152.85 U mL-1. Thermal and pH stability assays with the crude extract showed that more than 60 % of the activity remained at pH 4.6 and 60 °C, even after an exposition to these conditions longer than 24 h. Yet, after purification, the enzyme was stable at these for at least 4 h, which indicated that its purification for use in starch saccharification was...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Glucoamylase; Aspergillus niger; Solid-state fermentation; Biochemical characterization; Purification.
Ano: 2011 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132011000300018
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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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