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  • 1
    Electronic Resource
    Electronic Resource
    Optimization for xylanase and cellulase production from Aspergillus niger ATTC 6275 in palm oil mill wastes and its application (1997)
    Springer
    World journal of microbiology and biotechnology 13 (1997), S. 555-559 
    Details
    ISSN: 1573-0972
    Keywords: Aspergillus niger ; cellulase ; optimization ; palm oil wastes ; xylanase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Optimization of enzyme production from Aspergillus niger ATCC 6275 under both submerged and solid-substrate cultivation was investigated. Results from submerged cultivation using palm oil mill effluent revealed that pretreatment of ground palm cake did not improve enzyme production. Addition of 0.60g NH4NO3/l generated maximum activity of xylanase and cellulase (CMCase). The optimum aeration rate was 1.2 v/v min. Under solid-substrate cultivation, the results indicated that heating and alkali treatment of the ground palm cake gave no further improvement in enzyme production. The optimal N-source was 2% urea. Optimal initial moisture contents for xylanase and CMCase activities were 60% and 50% respectively, with temperature optima of 30°C and 35°C, respectively. The optimal inoculum size was 1× 108 spores/g palm cake with an initial pH of 4.5–5.0. The maximum activities of xylanase (282.9U/g) and CMCase (23.8U/g) were obtained under the optimum conditions. Solid-substrate cultivation was a better method for the production of enzyme, particularly xylanase, from A. niger ATCC 6275. The application of these enzymes to decanter effluent showed the separation of oil and grease and suspended solids from the effluent. This is comparable to the result achieved from using the commercial xylase preparation Meicelase and superior to the effect of Sumyzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018569426594
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  • 2
    Electronic Resource
    Electronic Resource
    The theory of everything and molecular evolution (1997)
    Springer
    World journal of microbiology and biotechnology 14 (1997), S. 171-176 
    Details
    ISSN: 1573-0972
    Keywords: Bacteria ; DNA ; evolution ; molecular ; optimization ; RNA ; theory ; time
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The theory of everything is discussed in relationship to early bacterial molecular evolution. The emphasis is on time, space (or location at the molecular level), the universal construction kit (elements contained in periodic table) and change per units of time that were necessary for early bacterial molecular evolution to occur.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008817726536
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  • 3
    Electronic Resource
    Electronic Resource
    Production and properties of a cellobiose-oxidizing enzyme from a newly isolatedcellulolytic bacterium Cytophaga sp. LX-7 (1997)
    Springer
    World journal of microbiology and biotechnology 13 (1997), S. 683-688 
    Details
    ISSN: 1573-0972
    Keywords: C ellobiose-oxidizing enzyme ; Cytophaga sp ; optimization ; production
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract A cell-bound cellobiose-oxidizing enzyme was produced by cellulolytic Cytophaga sp. LX-7. It was found that both the cellulosic substrates and the soluble carbohydrate substrates tested promoted the production of the cellobiose-oxidizing enzyme, and the highest specific activities were obtained with cellulose powder MN300, carboxy- methylcellulose CM22, maltose and cellobiose. Among the nitrogen sources examined, peptone gave the best cellobiose-oxidizing enzyme production, whereas inorganic nitrogen sources gave very poor growth. The medium buffered with Tris/HCl, pH 7.1, yielded the highest levels of cellobiose-oxidizing enzyme activity and the temperature optimum for crude enzyme activity was 40°C.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018527106547
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