Cellulose and xylan degrading enzymes ofFusarium avenaceum
✍ Scribed by Jadwiga Zalewska-Sobczak; Henryk Urbanek
- Book ID
- 104770135
- Publisher
- Springer
- Year
- 1981
- Tongue
- English
- Weight
- 461 KB
- Volume
- 129
- Category
- Article
- ISSN
- 0302-8933
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✦ Synopsis
It was found that crude preparation obtained from the culture medium of Fusarium avenaceum degraded cellulose and xylan. After chromatography on CM-Sepharose CL-6B of this preparation six fraction were obtained. The eluted fractions II and V showed xylanase activity, fraction IV cellulase activity and fraction III-xylanase and cellulase activity. The end products of xylan hydrolysis by all xylanase fractions (II, III, V) were xylobiose, xylose, xylotriose and xylotetrose. The end products of cellulose hydrolysis by fractions III and IV was cellobiose, glucose and cellotriose.
The data from gel filtration on Sephacryl S-200 indicated a molecular weight of more than 250,000 for both cellulase IV and xylanase V. After gel filtration in the presence of urea disaggregafion of those high molecular xylanase and cellulase particles was observed. Xylanase II in difference from the other fractions contained higher amount of sugar. Digestion of fraction II with cellulase-hemicellulase preparation from Phoma hibernica decreased the content of sugar from 17 ~ to 8 ~, but did not change its enzymatic properties. Cellulase IV as well as x3(lanase V were inactivated by N-bromosuccinimide, 2-hydroxy-5-nitrobenzyl bromide and tetranitromethane, hence it is suggested that tryptophan and tyrosine are the essential for the activity of these enzymes.
📜 SIMILAR VOLUMES
## Abstract Degradation of xylan requires several enzymes. Two chimeric enzymes, xyln–ara and xyln–xylo, were constructed by linking the catalytic portion of a xylanase (xyln) to either an arabinofuranosidase (ara) or a xylosidase (xylo) with a flexible peptide linker. The recombinant parental enzy