Angelo R, Aguirre C, Curotto E, Esposito E, Fontana J D, Baron M, Milagres A M, Durán N
Instituto de Quimica, Universidade Estadual de Campinas, S.P., Brazil.
Biotechnol Appl Biochem. 1997 Feb;25(1):19-27. doi: 10.1111/j.1470-8744.1997.tb00410.x.
The 2M1 strain of Aspergillus sp., which showed high extracellular xylanolytic activities in a pre-screening, was studied. Oat-spelt, birch, eucalyptus and pine xylans were used as xylanolytic inductors. The following activities were found at 50 degrees C in the presence of 1% xylan: 120 units/ml (oat-spelt xylan), 132 units/ml (birch xylan), 107 units/ml (eucalyptus xylan), 67 units/ml (pine xylan) and 137 units/ml (larch-wood xylan). Xylanase induced by pine xylan exhibited a higher stability than those induced by the other xylans. The stability was improved by addition of glycerol. In the crude extract, reagents which were found to affect xylanase activity were 1-ethyl-3-(3-dimethylaminopropyl)carbodi-imide for amidation of carboxylic groups and N-bromosuccinimide at a concentration of 0.5 mM for indole oxidation. Methylene Blue, butane-2,3-dione, N-acetylimidazole, chloramine-T and iodoacetate had little effect on the enzyme activity (more than 97% of the original activity remained).