Library

X
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
    A simple method of affinity chromatography for the purification of glucoamylase obtained from Aspergillus niger C
    Amsterdam : Elsevier
    FEBS Letters 149 (1982), S. 63-66 
    Details
    ISSN: 0014-5793
    Keywords: (Aspergillus niger C) ; Affinity chromatography ; Characterization ; Exosplitting enzyme ; Glucoamylase purification ; Purification, large scale
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(82)81072-7
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Changes of the affinity between fungal proteins and vanillin bonded to thermally modified porous glass support (1984)
    Springer
    Chromatographia 18 (1984), S. 41-43 
    Details
    ISSN: 1612-1112
    Keywords: Affinity chromatography ; Proteins affinity to vanillin ; Controlled porosity glass ; Thermally modified glass support ; Boron enriched glass surface
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary The affinity of peroxidase and the fungal proteins to vanillin attached to controlled porous glasses depends on the porosity of the glass and additional thermal treatment of the support. The additional thermal treatment of controlled porous glasses leads to an enrichment in boron atoms of their surface. The results presented in this paper show a better resolution of the analyzed substances when glass with a surface enriched in boron was used as the support for vanillin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02279464
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Influence of the thermal modification of controlled porosity glass on the affinity chromatography of fungal proteins (1984)
    Springer
    Chromatographia 18 (1984), S. 389-392 
    Details
    ISSN: 1612-1112
    Keywords: Controlled porous glasses ; Separation of fungal proteins ; Affinity chromatography ; Trametes versicolor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary The properties and the coverage density of chemically bonded phases depend among others on the properties of their supports. Controlled-porosity glasses (CPG) are materials used as a support of bio-active ligands. Their network mainly consist of SiO2 as well as of a small amount of B2O3 and Na2O. The characteristic feature of porous glasses is the possibility of a change in the surface boron concentration leading to the change of the properties of their surface. This paper deals with the results of the separation of fungal proteins on packings consisting of vanillin bonded to CPG with different boron concentration on its surface. It appears from the data obtained that the changes in the affinity of the fungal proteins to the packing are related to the extend of the thermal treatment of the CPG. The protein fractions separated by chromatography were confirmed to be homogeneous by poly-acryloamide gel disc electrophoresis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02262487
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    The purification and immobilization of Penicillium notatum β-galactosidase (1995)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 15 (1995), S. 211-222 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Penicillium notatum No. 1 as a producer of β-galactosidase was cultivated in a 5-1 fermenter. Various methods of protein isolation and concentration from the culture fluid were optimized. Then the conditions of β-galactosidase purification using an affinity chromatographic technique were established. The purified enzyme was immobilized on a controlled porous glass (CPG). The optimum temperature and pH values of the native and immobilized forms of β-galactosidase were determined as 50°C and 30-50°C as well as pH 3 and pH 3-5, respectively.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370150211
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Influence of the mycelium growth conditions on the production of amylolytic, proteolytic and pectinolytic enzymes by Aspergillus niger C (1989)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 9 (1989), S. 355-361 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Various nitrogen and carbon sources, as well as natural products, were examined as inducers of the production of amylases, proteases and pectinases by A. niger C. A. niger C grown on wheat bran extract medium provided culture supernatants with the highest enzymatic activities. Some culture conditions, e.g. pH, medium temperature and time period of cultivation, were optimalized to improve the growth and enzymes biosynthesis by A. niger C.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370090411
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Immobilization of fungal peroxidase on alkylaminated organic and inorganic porous supports (1988)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 8 (1988), S. 47-53 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Several alkylaminated porous silica gels and acrylic type porous polymers have been used for covalent binding of fungal peroxidase from Trametes versicolor. The immobilization efficiency expressed in terms of the bound protein content, specific enzyme activity, and enzyme storage stability have been determined for both types of supports used. The results indicate a better immobilization ability of organic polymers in comparison with silica gels.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370080108
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Immobilization of enzymes on porous silica supports (1989)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 9 (1989), S. 239-246 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Four silica supports differing in pore dimensions were activated by treatment with SiCl4 and then with ethylenediamine to obtain alkylamine groups on the silica surface. Three enzymes, peroxidase from cabbage, glucoamylase from Aspergillus niger C and urease from soybean were immobilized on these supports using glutaraldehyde as coupling agent. It was found that the protein content, the retained enzymatic activity and the storage stability of the silica supported enzymes were considerably affected by support pore size and enzyme molecular weight, the factors which are supposed to alter protein distribution inside the support pores. The highest activity was found for peroxidase and glucoamylase attached to the silica with the widest pores, but their loss in activity during storage was considerable. The urease retained less activity after immobilization, but its storage stability was excellent.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370090310
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...