Please use this identifier to cite or link to this item: http://localhost:8080/xmlui/handle/123456789/2061
Title: Permeabilization and inhibition of the germination of spores of Aspergillus niger for gluconic acid production from glucose
Authors: Sumitra, R
Fontanille, P
Pandey, A
Larroche, C
Keywords: Aspergillus niger spores
Glucose oxidase
Gluconic acid
Sodium azide
Issue Date: 2008
Publisher: Elsevier
Citation: Bioresource Technology 99(11):4559-4565;Jul 2008
Abstract: In this study, the role of citral to permeabilize the spores of Aspergillus niger and replace sodium azide in the bioconversion medium was studied. Further, characterization of glucose oxidase of spores was carried out by exposing both permeabilized and unpermeabilized spores to different pressures (1, 2, 2.7 kb) and temperatures (60, 70, 80, 90 degrees C). Unpermeabilized spores after exposure to high temperatures were permeabilized by freezing before using as catalyst in the bioconversion reaction. Results showed that citral permeabilized the spores and could inhibit spore germination in the bioconversion medium. Rate of reaction was significantly increased from 1.5 to 4.35 g/L h which was higher than the commercial glucose oxidase 2 g/L h). Glucose oxidase activity of A. niger was resistant to pressure. However, pressure treatment could not permeabilize them. Behaviour of fresh and permeabilized spores to temperature varied significantly. Glucose oxidase activity of fresh spores exposed to high temperature was unaffected at 70 degrees C till 15 min and 84% of relative activity was retained even after 1 h at 70 degrees C while permeabilized spore got inactivated at 70 degrees C for 15 min, which followed the same pattern as commercial glucose oxidase. Cellular membrane integrity was lost due to permeabilization by freezing which resulted in heat-inactivation of glucose oxidase when spores were permeabilized before heat treatment. Thus, glucose oxidase of spore remains heat stable when unpermeabilized and active while permeabilized and its reaction rate is higher than the commercial glucose oxidase.
URI: http://ir.niist.res.in:8080/jspui/handle/123456789/2061
ISSN: 0960-8524
Appears in Collections:2008

Files in This Item:
File Description SizeFormat 
2008_0136.PDF
  Restricted Access
324.63 kBAdobe PDFView/Open Request a copy


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.