Enhanced stability of cellulase-free xylanase from Chainia sp. (NCL 82.5.1)

Chainia sp. (NCL 82.5.1) produces an extracellular, cellulase-free xylanase. The ready accessibility of the enzyme to cellulose pulp due to its small size and the absence of cellulase are advantageous features. The enzyme is stable at 40 degrees C for 1h and in a PH range of 5-9 at 4 degrees C. Impr...

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Bibliographic Details
Published in:Biotechnology letters 1994-02, Vol.16 (2), p.179-182
Main Authors: Bandivadekar, K.R, Deshpande, V.V
Format: Article
Language:English
Subjects:
Actinomycetales
additives
Biological and medical sciences
Biotechnology
blanching
Chainia
Enzyme engineering
Fermentation
Fundamental and applied biological sciences. Psychology
heat stability
Methods. Procedures. Technologies
O-glycoside hydrolases
ph stability
Production of selected enzymes
stability
temperature
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Summary:Chainia sp. (NCL 82.5.1) produces an extracellular, cellulase-free xylanase. The ready accessibility of the enzyme to cellulose pulp due to its small size and the absence of cellulase are advantageous features. The enzyme is stable at 40 degrees C for 1h and in a PH range of 5-9 at 4 degrees C. Improved stability of the enzyme at higher temperature and pH are desirable. Effect of a variety of compounds was studied to enhance stability. Glycerol, sorbitol, mannitol (10%) or glycine (1M) had marginal effect on thermostability. Addition of Ca+2 or PEG (10 mM) increased the half-life of the enzyme at 60 degrees C. Cysteine (10 mM) or Tween-80 (1%) showed 70% protection against thermal inactivation. Xylan (3%) offered complete protection against inactivation of the enzyme at 60 degrees C and at pH 9.
ISSN:0141-5492
1573-6776
DOI:10.1007/BF01021667