Library

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Biology and fertility of soils 25 (1997), S. 1-6 
    ISSN: 1432-0789
    Keywords: Key words Tillage ; Soil enzymes ; Microbial biomass ; Dehydrogenase activity ; Nucleic acids ; Farming practices
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Geosciences , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Modification of soil environment by different farming practices can significantly affect crop growth. Tillage causes soil disturbance, altering the vertical distribution of soil organic matter and plant nutrient supplies in the soil surface, and it may affect the enzyme activity and microbial biomass which are responsible for transformation and cycling of organic matter and plant nutrients. In this study, the influence of three conventional tillage systems (shallow plowing, deep plowing and scarification) at different depths on the distribution and activity of enzymes, microbial biomass and nucleic acids in a cropped soil was investigated. Analysis of variance for depth and tillage showed the influence of the different tillage practices on the activity of some enzymes and on the nucleic acids. Glucosidase, galactosidase, nitrate reductase and dehydrogenase activity were significantly affected by the three tillage modalities. Activity in the upper layer (0–20 cm) was higher in the plots tilled by shallow plowing and scarification than in those tilled by deep plowing. Positive relationships were observed between the soil enzymes themselves, with the exception of urease and pyrophosphatase activity. Moreover, significant correlations were found between DNA and β-galactosidase, and between RNA and β-glucosidase, β-galactosidase, alkaline phosphatase and phosphodiesterase. α-Glucosidase, β-galactosidase, alkaline phosphatase and phosphodiesterase were highly correlated with biomass C determined by the fumigation-extraction method.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochemical and Biophysical Research Communications 149 (1987), S. 807-814 
    ISSN: 0006-291X
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 3
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Phytochemistry 22 (1983), S. 1885-1889 
    ISSN: 0031-9422
    Keywords: Gramineae ; MW ; Triticum aestivum ; amino acid composition ; copper content ; inhibitors. ; isoenzyme ; kinetic properties ; o-diphenolase ; wheat
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 48 (1995), S. 585-591 
    ISSN: 0006-3592
    Keywords: phenoloxidases ; enzyme immobilization ; reverse micelles ; organic gels ; biotic detoxification ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Gelatine gels originate from water in oil microemulsions in which the ternary system consists of isooctane/ sulfosuccinic acid bis [2-ethyl hexyl] ester/water; the solubilization of gelatin in the water pool of these microemulsions transforms them into viscous gels in which it is possible to cosolubilize various reactive molecules. These gels were used to immobilize two phenoloxidases, a laccase from Trametes versicolor and a tyrosinase from mushroom. The best balance between gel retention and catalytic activity was reached at a gelatine concentration of 2.5% (w/v) in the case of tyrosinase, while laccase immobilization was independent of gelatine concentration. Both enzymes kept the same optimum pH as the corresponding soluble controls, while a partial loss of activity was observed when they were immobilized. Immobilized enzymes showed an increased stability when incubated for several days at 4°C with a very low release from the gels in the incubation solutions. The immobilization of tyrosinase and of laccase enhanced stability to thermal inactivation. Furthermore, gel-entrapped tyrosinase was almost completely preserved from proteolysis: more than 80% of the activity was maintained, while only 25% of the soluble control activity was detected after the same proteolytic treatments. A column packed with gel-immobilized tyrosinase was used to demonstrate that enzymes immobilized with this technique may be reused several times in the same reaction without loosing their efficiency. Finally, gel-entrapped tyrosinase and laccase were capable of removing naturally occurring and xeno-biotic aromatic compounds from aqueous suspensions with different degrees of efficiency. © 1995 John Wiley & Sons, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...