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Moreira,Fabiana G.; Lenartovicz,Veridiana; Souza,Cristina G.M. de; Ramos,Edivan P.; Peralta,Rosane M.. |
The use of a methyl-D-glucoside (alphaMG), a synthetic analogue of maltose, as carbon source and inducer of amylase synthesis to several species of Aspergillus was studied in submerged and solid-state fermentations. Among a group of ten species, A. tamarii, A. fumigatus and A. flavus were able to produce biomass and high specific amylolytic activity in submerged cultures containing alphaMG as the only carbon source. In solid state fermentation, the enrichment of basal wheat bran or corn cob medium with alphaMG increased up to 3 times the production of amylases. In both submerged and solid state fermentations, alphaMG was more effective inducer of amylases than maltose and starch. |
Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Amylase; Aspergillus; Solid-state fermentation; Submerged fermentation. |
Ano: 2001 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822001000100004 |
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Moreira,Fabiana Guillen; Lima,Francieli Arrias de; Pedrinho,Sophia Renata Fazzano; Lenartovicz,Veridiana; Souza,Cristina Giatti Marques de; Peralta,Rosane Marina. |
A strain of Aspergillus tamarii, a filamentous fungus isolated from soil, was able to produce both <FONT FACE="Symbol">a</FONT>-amylase and glucoamylase activities in mineral media supplemented with 1% (w/v) starch or maltose as the carbon source. Static cultivation led to significantly higher yields than those obtained using shaking culture. The production of amylases was tolerant to a wide range of initial culture pH values (from 4 to 10) and temperature (from 25 to 42oC). Two amylases, one <FONT FACE="Symbol">a</FONT>-amylase and one glucoamylase, were separated by ion exchange chromatography. Both partially purified enzymes had optimal activities at pH values between 4.5 and 6.0 and were stable under acid conditions (pH... |
Tipo: Info:eu-repo/semantics/article |
Palavras-chave: < FONT FACE=Symbol> A< /FONT> -amylase Aspergillus tamarii glucoamylase. |
Ano: 1999 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37141999000200014 |
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