Occurrence of a thermoacidophilic cell-bound exo-pectinase inAlicyclobacillus acidocaldarius

Alicyclobacillus acidocaldarius was able to degrade pectin under thermoacidophilic conditions of high temperature and acidity. Both extracellular and cell-bound pectolytic activities were found (28 and 72% of total activity, respectively). WhenA. acidocaldarius was subjected to lysozyme or sonicatio...

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Bibliographic Details
Published in:Folia microbiologica 1998-12, Vol.43 (6), p.657-660
Main Authors: Ordoñez, R. G., Morlon-Guyot, J., Gasparian, S., Guyot, J. P.
Format: Article
Language:English
Subjects:
Acidity
Gel electrophoresis
High temperature
Lysozyme
Pectin
Pectinase
Sodium lauryl sulfate
Sonication
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Summary:Alicyclobacillus acidocaldarius was able to degrade pectin under thermoacidophilic conditions of high temperature and acidity. Both extracellular and cell-bound pectolytic activities were found (28 and 72% of total activity, respectively). WhenA. acidocaldarius was subjected to lysozyme or sonication, more than 50% of the activity was found to be bound with the cell debris. The cell-bound enzyme presented principally exopectolytic activity. SDS-PAGE and zymogram showed that the estimated molar mass of the crude enzyme was 52 kDa. pH optimum was between 1.5 and 2.0 and the enzyme was thermostable at 70°C for 1 h at pH 2.0.
ISSN:0015-5632
1874-9356
DOI:10.1007/BF02816385