ISSN:
0006-3592
Keywords:
Aspergillus awamori
;
low protease production
;
dinitrosalicylic method
;
xylanase
;
β-xylosidase
;
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
A growth medium was developed for maximal production in batch culture of extracellular xylanase and β-xylosidase by Aspergillus awamori CMI 142717 and a mutant (AANTG 43) derived from the wild-type strain. The optimum pH for the production of xylanase and β-xylosidase was 4.0. The best temperature of xylanase production was 30°C; 35°C was optimal for β-xylosidase. Protease production was never completely suppressed under any of the conditions tested. However, protease titre was 3.5-fold less than the control in medium in which proteose peptone and yeast extract were omitted: the level of xylanase was not affected (8.6 U mL-1) but β-xylosidase titre was increased 4.7-fold to 1.5 U mL-1. When corn steep liquor was used as the sole nitrogen source, xylanse and β-xylosidase titres were further increased by 1.5- and 1.9-fold, respectively. Of the carbon sources investigated, ball-milled oat straw or oat spelt xylan produced the highest titres of xylanse and β-xylosidase. None of the soluble carbon sources investigated produced the high titres of xylanase or β-xylosidase induced by either oat straw for xylanse and β-xylosidase was 2% and the optimum spore inoculum was between 106 and 107 spores/mL-1 final concentration. The level of xylanse activity obtained in the culture filtrates of the mutant was a remarkable 820 U mL-1 when the reducing sugar released was measured by the dinitrosalicylic acid method. This enzyme titre would appear to be the highest reported so far. The xylanases system contained the correct balance of enzymes to effect extensive hydrolysis of oat spelt xylan. The protease titre was very low.
Additional Material:
2 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/bit.260380810
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