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
Filter
  • fluorodinitrobenzene  (1)
  • immobilized digestive enzyme assay (IDEA)  (1)
  • streptavidin  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Digestibilities of the protein in various foods as determinedin vitro by an immobilized digestive enzyme assay (IDEA) (1989)
    Springer
    Plant foods for human nutrition 39 (1989), S. 59-65 
    Details
    ISSN: 1573-9104
    Keywords: immobilized digestive enzyme assay (IDEA) ; protein digestibility
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract The digestibility of the protein in various foods or food components was analyzed using an immobilized digestive enzyme assay (IDEA) system. The assay consists of two bioreactors, one containing pepsin and the other containing trypsin, chymotrypsin and intestinal mucosa peptidases. The fraction of the peptide bonds hydrolyzed during an extent of hydrolysis assay was correlated with independentin vivo determinations of the digestibilities. A correlation coefficient of 0.80 was obtained. The derived linear regression equation can be used to predict digestibility. The method is sensitive to structural modification of protein, as for example, those caused by effects of heat treatment.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01092402
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    The estimation of ‘available lysine’ in human foods by three chemical procedures (1989)
    Springer
    Plant foods for human nutrition 39 (1989), S. 129-135 
    Details
    ISSN: 1573-9104
    Keywords: lysine ; reactive lysine ; protein foods ; fluorodinitrobenzene ; o-phthalaldehyde ; dye-binding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Seventeen test foods were each analyzed by four methods. Total lysine was measured by conventional amino acid analysis. Reactive lysine was measured with either fluorodinitrobenzene, o-phthalaldehyde or a differential dye-binding procedure. The results were then compared with another group's results from rat growth assays of the same samples for availably lysine. A sample of deliberately heat-damaged milk powder gave a rat assay value corresponding to 64% of its total lysine content; other values were all higher and on average 99% for 7 animal products, and 87% for 9 vegetable products. The correlation coefficient between the two sets of values was 0.95. The ‘reactive lysine’ procedures failed to give a better prediction of the rat values.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01092409
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    An Escherichia coli plasmid vector system for production of streptavidin fusion proteins: Expression and bioselective adsorption of streptavidin-β-galactosidase (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 44 (1994), S. 1348-1354 
    Details
    ISSN: 0006-3592
    Keywords: streptavidin ; galactosidase ; fusion proteins ; plasmid vector ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Covalently immobilized biotin was used as a biospecific adsorbant to investigate the application of streptavidin as an affinity domain for simultaneous purification and immobilization of recombinant proteins. A streptavidin-β-galactosidase fusion protein was constructed and tested as a model system. The gene for streptavidin from Streptomyces avidinii was modified by polymerase chain reaction to mutate the stop codon and to facilitate cloning into an Escherichia coli expression vector yielding a versatile plasmid with 37 unique restriction enzyme sites at the 3' end. E. coli β-galactosidase was cloned in-frame to the streptavidin gene. Analysis of lysates of induced recombinant E. coli cells by SDS-PAGE and Western blots indicated that the 133.6-kDa fusion protein was expressed. Sulfosuccinimidyl-6-(biotinamido) hexanoate was covalently immobilized on 3-aminopropyl-controled-pore glass beads. Exposure of recombinant cell lysates to this support indicated that streptavidin-β-galactosidase was bioselectively adsorbed. The resulting biocatalyst contained 300 mg protein per gram of beads and exhibited a specific activity of 306 βmol/min per milligram protein with o-nitrophenyl-β-D-galactopyranoside as substrate corresponding to approximately 50% of that observed for commercially pure E. coli β-galactosidase. © 1994 John Wiley & Sons, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260441111
    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...