Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/5751
Title: Partial purification and characterization of <img src='/image/spc_char/alpha.gif'> -amylase produced by <i style="">Aspergillus oryzae</i> using spent-brewing grains
Authors: Patel, Anil Kumar
Nampoothiri, K Madhavan
Ramachandran, Sumitra
Szakacs, George
Pandey, Ashok
Keywords: <img src='/image/spc_char/alpha.gif'> -Amylase
<i style="">Aspergillus oryzae</i>
solid-state fermentation
spent brewing grains
Issue Date: Jul-2005
Publisher: CSIR
Series/Report no.: Int. Cl.<sup>7</sup> A01N63/02; C12N9/30; C12R1: 69
Abstract: Solid-state fermentation (SSF) was carried out to produce <img src='/image/spc_char/alpha.gif'> -amylase from <i style="">Aspergillus oryzae</i> (IFO 30103) using spent brewing grains (SBG) as substrate. A maximum of 11296 U/gds amylase activity was obtained after 48 h of fermentation. The extracted enzyme was subjected to partial purification by ammonium sulphate fractionation. Maximum specific activity was obtained with 40-70% fraction. SDS-PAGE of the corresponding sample revealed an approximate 66 kDa band, which was confirmed by activity staining as <img src='/image/spc_char/alpha.gif'> -amylase. It was optimally active at <i style="">p</i>H 5 and 50°C by using 1% starch as substrate concentration. The partially purified <img src='/image/spc_char/alpha.gif'> -amylase loses activity rapidly above 50<sup>o</sup>C but it can be retained in the presence of Ca<sup>2+</sup>. Presence of Mn<sup>2+</sup> and Fe<sup>2+</sup> enhanced the enzyme activity and is almost doubled in presence of Mn<sup>2+</sup>. However, in the presence of Hg<sup>2+</sup> and Cu<sup>2+,</sup> the activity is reduced. Hg<sup>2+</sup> reduced the enzyme activity by half.
Description: 336-341
URI: http://hdl.handle.net/123456789/5751
ISSN: 0975-0967 (Online); 0972-5849 (Print)
Appears in Collections:IJBT Vol.04(3) [July 2005]

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