Purification and cellulosomal localization ofClostridium thermocellummixed linkage β-glucanase LicB (1,3–1,4-β-D-glucanase)
✍ Scribed by V. V. Zverlov; K. P. Fuchs; W. H. Schwarz; G. A. Velikodvorskaya
- Publisher
- Springer Netherlands
- Year
- 1994
- Tongue
- English
- Weight
- 581 KB
- Volume
- 16
- Category
- Article
- ISSN
- 0141-5492
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
A P-D-glucan isolated from a Japanese marine alga known as "Arame" (Eisenia bicyclis) was shown by methylation analysis to be composed of (l-3) and (l-+6) linkages and ( 1+3),(1+6) branch points. The 13C-n.m.r. spectrum confirmed these linkages and also verified the absence of /3-( l-+4) linkages. T
An enzyme active against 0-(carboxymethyl)cellulose (CMC) was purified from a synthetic medium containing ball-milled cellulose wherein Ruminococcus albus had been cultivated for 70 h. After 570-fold purification, a homogeneous enzyme was obtained in a yield of 3%. The enzyme degraded CMC (molecular
## Abstract **BACKGROUND:** 1,3‐1,4‐β‐D‐glucanase (1,3‐1,4‐β‐D‐glucan 4‐glucanohydrolase; EC 3.2.1.73) has been used in a range of industrial processes. As a biocatalyst, it is better to use immobilized enzymes than free enzymes, therefore, the immobilization of 1,3‐1,4‐β‐D‐glucanase was investigat