ENHANCED STABILITY OF CELLULASE-FREE XYLANASE FROM CHAINIA SP (NCL-82.5.1)

Citation
Kr. Bandivadekar et Vv. Deshpande, ENHANCED STABILITY OF CELLULASE-FREE XYLANASE FROM CHAINIA SP (NCL-82.5.1), Biotechnology letters, 16(2), 1994, pp. 179-182
Citations number
5
Categorie Soggetti
Biothechnology & Applied Migrobiology
Journal title
ISSN journal
01415492
Volume
16
Issue
2
Year of publication
1994
Pages
179 - 182
Database
ISI
SICI code
0141-5492(1994)16:2<179:ESOCXF>2.0.ZU;2-D
Abstract
Chainia sp. (NCL 82.5.1) produces an extracellular, cellulase-free xyl anase. 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 (10mM ) increased the half-life of the enzyme at 60 degrees C. Cysteine (10m M) or Tween-80 (1%) showed 70% protection against thermal inactivation . Xylan (3%) offered complete protection against inactivation of the e mzyme at 60 degrees C and at pH 9.