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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    World journal of microbiology and biotechnology 16 (2000), S. 373-376 
    ISSN: 1573-0972
    Keywords: Ectomycorrhizal fungi ; freeze-drying ; nitrate reductase ; nuclease ; pectinase ; protease ; qualitative enzyme assay
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Qualitative enzyme assays were used as a tool to investigate the stability of freeze-dried mycorrhizal fungi. Both lyophilized (L) and non-lyophilized (NL) mycelia of individual isolates showed identical response for all the enzymes tested (nitrate reductase, protease, pectinase, and nuclease). All the isolates showed positive nitrate reductase activity, except two isolates of Thelephora terrestris (both L and NL). Both L and NL cultures of individual isolates showed substrate specificity (between gelatin and casein) for protease activity. Though both L and NL mycelia of all the culture isolates grew upon pectin substrate, there was no pectinase activity expressed. RNAase activity was variously exhibited (little activity, little growth–no activity, and no growth–no activity) by individual test cultures. The consistencies in growth and enzyme activity of the cultures before and after lyophilization imply the stability of the freeze-dried vegetative mycelium.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    World journal of microbiology and biotechnology 11 (1995), S. 242-243 
    ISSN: 1573-0972
    Keywords: Aspergillus sp. PK-7 ; isolation ; purification ; xylanase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract AnAspergillus sp., isolated from a rubbish dump, produced 10.6 IU ml-1 xylanase activity. Two xylanases were recognized and each was purified to homogeneity by two-stage chromatography on DEAE-and CM-Sepharose. Xylanase I had a pI of 7.2 and anM r of 26 kDa whereas xylanase II had a pI of 4.7 and anM r of 21 kDa. At 50°C, xylanase I was stable for 2.5 h but xylanase II was only stable for 1 h.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    World journal of microbiology and biotechnology 16 (2000), S. 865-868 
    ISSN: 1573-0972
    Keywords: Amylase ; cellulase ; ectomycorrhizal fungi ; β-glucosidase ; lignin degrading enzymes ; lipase ; lyophilization ; urease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Freeze-dried ectomycorrhizal fungus cultures were tested for qualitative enzymatic activity and compared with that of the non-lyophilized culture. Enzymes involved in the utilization of starch, cellulose, lipid, lignin and urea were tested for their qualitative presence/activity. Expression of amylase and urease was stronger than that of lipase and lignin-degrading activity for the isolates tested. Variation among the species of Laccaria was low and prominently seen only for cellulase and urease. Amanita muscaria showed significant variation relative to other members of the Agaricales reported in the present study, except for β-glucosidase activity. All the enzymatic tests showed an unequivocal uniformity between the lyophilized vegetative mycelium (L) and the respective non-lyophilized mycelial cultures (NL), indicating that the lyophilization procedure maintained stable enzyme activity.
    Type of Medium: Electronic Resource
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  • 4
    Publication Date: 2017-10-03
    Print ISSN: 0170-0839
    Electronic ISSN: 1436-2449
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Published by Springer
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