Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UMLS:C0040822 (
tremor
)
18,428
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Enzyme stability studies in case of Sclerotium rolfsii UV-8 mutant have been investigated under the conditions used for saccharification of cellulose (50 degrees C, pH 4.5, 48 h). Avicelase (measure of exoenzymes) and xylanase were found to be less stable than CMCase (endoglucanase) and
beta-glucosidase
. Merthiolate (and other Hg compounds) added as a biocide, inactivated avicelase and xylanase about 60-70%. Of the antibiotics tested, tetracycline, chloramphenicol, and streptomycin sulfate were found suitable as an additive in cellulose hydrolysis system. The optimum hydrolysis of alkali-treated (AT)-rice straw, AT-bagasse, Solka Floc SW40, and Avicel P.H.101 was observed under
shaking
conditions at pH 4.5, 50 degrees C in CO2 atmosphere. It is suggested, all the studied parameters could be used for the evaluation of mutant strains.
...
PMID:Factors affecting stability of Sclerotium rolfsii UV-8 mutant cellulase complex under saccharification conditions. 179 12
The efficient saccharification of lignocellulosic materials requires the cooperative actions of different cellulase enzyme activities: exoglucanase, endoglucanase,
beta-glucosidase
, and xylanase. Previous studies with the fungi strains Aureobasidium sp. CHTE-18, Penicillium sp. CH-TE-001, and Aspergillus terreus CH-TE-013, selected mainly because of their different cellulolytic and xylanolytic activities, have demonstrated the capacity of culture filtrates of cross-synergistic action in the saccharification of native sugarcane bagasse pith. In an attempt to improve the enzymatic hydrolysis of different cellulosic materials, we investigated a coculture fermentation with two of these strains to enhance the production of cellulases and xylanases. The 48-h batch experimental results showed that the mixed culture of Penicillium sp. CH-TE-001 and A. terreus CH-TE-013 produced culture filtrates with high protein content, cellulase (mainly
beta-glucosidase
), and xylanase activities compared with the individual culture of each strain. The same culture conditions were used in a simple medium with mineral salts, corn syrup liquor, and sugarcane bagasse pith as the sole carbon source with moderate
shaking
at 29 degrees C. Finally, we compared the effect of the cell-free culture filtrates obtained from the mixed and single fermentations on the saccharification of different kinds of cellulosic materials.
...
PMID:Mixed submerged fermentation with two filamentous fungi for cellulolytic and xylanolytic enzyme production. 1201 34
A simple extraction procedure was applied to the analysis of canned/packaged white nuts and Ginkgo biloba extracts. Extraction by
shaking
with water at room temperature was more convenient to use than a previously published Soxhlet procedure for analysis of packaged Ginkgo biloba seeds (white nuts) for ginkgotoxin; recoveries from spiked dried seeds by the simple extraction procedure averaged 76%. Determination was by liquid chromatography with UV or fluorescence detection. Recoveries of ginkgotoxin from a spiked and unspiked natural health product (powder from Ginkgo biloba capsules) were equivalent by both procedures; recovery from spiked powder by the simple extraction procedure was 81%. Application of this extraction procedure in the analysis of 6 samples of white nuts (vacuum packaged and canned products) showed that free ginkgotoxin was present in 5 samples at concentrations up to 25 microg/g dry weight. Total ginkgotoxin was determined after hydrolysis with
beta-glucosidase
of sample extracts in which a peak corresponding to the 5'-O-glucoside was detected. Ginkgotoxin was determined in 10 Ginkgo biloba natural health products by the same method at levels up to 181 microg/g.
...
PMID:Improved extraction of ginkgotoxin (4'-O-methylpyridoxine) from Ginkgo biloba products. 1575 22