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Influence of agitation speeds and aeration rates on the Xylanase activity of Aspergillus niger SS7 BABT
Bakri,Yasser; Mekaeel,Alaa; Koreih,Amal.
In this study, the effect of agitation and aeration rates on xylanase activity of Aspergillus niger SS7 in 3-litre stirred tank bioreactor was investigated. The agitation rates tested were 100, 200 and 300 rpm at each airflow rates of 0.5, 1.0 and 1.5 vvm. The maximum xylanase activity in mono- agitator system was at the agitation speed of 200 rpm and aeration rate of 1.0 vvm. In bi-agitator system, at low agitation speed (100 rpm), the xylanase activity was enhanced by 13% compared to mono- agitator system for an aeration rate of 1.0 vvm. Xylanase productivity in continuous culture was higher by approximately 3.5 times than in batch culture.
Tipo: Info:eu-repo/semantics/article Palavras-chave: Aspergillus niger; Agitation; Aeration; Xylanase.
Ano: 2011 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132011000400003
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Concomitant production of two proteases and alpha-amylase by a novel strain of Bacillus subtilis in a microprocessor controlled bioreactor BJM
Mukhtar,Hamid; Ikram-ul-Haq,.
We describe the simultaneous production of Bacillus subtilis based proteases and alpha amylase using a computer controlled laboratory scale 7.5 L batch bioreactor. The present strain is the first to be reported that concomitantly produces these two industrially important enzymes. The growth and sporulation of Bacillus subtilis was monitored and maximum production of alkaline protease and alpha amylase was found to coincide with maximum sporulation. Two types of proteases were detected in the fermentation broth; a neutral and an alkaline protease most active in a pH range of 7.0-8.0 and 8.0-10, respectively. Maximum production of proteases was observed at an incubation temperature of 37ºC while that of alpha amylase was observed at 40ºC. The optimum...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Simultaneous; Sporulation; Kinetics; Fermentation; Agitation.
Ano: 2012 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822012000300033
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